ABSTRACT
Protein electrophoresis (PEP) is an important tool in mammals to characterize specific dysproteinemias and detect acute and chronic inflammatory responses. In reptiles, PEP is the gold standard method for globulin fraction determination and albumin measurement. In this study, preliminary reference intervals were established for serum PEP in 22 clinically healthy adult Roti Island snake-necked turtles (Chelodina mccordi), a critically endangered species, kept in captivity and sampled over two monsoon seasons. The species has a prominent prealbumin fraction and ß-globulins were the dominant globulin fraction. Significant differences between females and males were found in prealbumin (P < 0.01), albumin (P = 0.02), α1-globulin (P = 0.05) and γ-globulin (P = 0.01). Gravid females had significantly lower total protein (P < 0.01), prealbumin (P < 0.01), albumin (P < 0.01) and albumin:globulin ratio (P = 0.01). These preliminary reference intervals should aid in clinical investigation in this species as well as further research studies seeking to understand the application of PEP in reptilian species.
Subject(s)
Blood Proteins , Turtles , Animals , Turtles/blood , Blood Proteins/analysis , Female , Reference Values , Male , Blood Protein Electrophoresis/veterinary , Blood Protein Electrophoresis/methods , Animals, Zoo/bloodABSTRACT
The white stork (Ciconia ciconia) is a ciconiiform species widely represented in zoological institutions. Plasma protein electrophoresis is widely used in avian patients for assessment of inflammatory conditions, but reference intervals for this testing modality are lacking for the white stork. The two main electrophoretic methods are agarose gel electrophoresis (AGE) and capillary zone electrophoresis (CZE). This study assessed fresh plasma samples of healthy adult white storks (n = 30). Statistical analyses were performed to evaluate agreement between AGE and CZE. Typical electrophoretic fractions were obtained from both methods (prealbumin, albumin, α1, α2, ß, γ1, and γ2). The AGE and CZE methods were not equivalent for determining major electrophoretic fractions (except ß-globulins) and albumin:globulin ratio on plasma samples. An additional prealbumin fraction was seen with CZE. Reference intervals were established for each method as the smallest n group was 27 individuals for a given value; most values had normal distribution, and robust or parametric methods were used on the data.
Subject(s)
Birds , Blood Proteins , Electrophoresis, Agar Gel , Electrophoresis, Capillary , Animals , Reference Values , Birds/blood , Blood Proteins/analysis , Electrophoresis, Capillary/veterinary , Electrophoresis, Capillary/methods , Electrophoresis, Agar Gel/veterinary , Female , Blood Protein Electrophoresis/veterinary , Blood Protein Electrophoresis/methods , MaleABSTRACT
While electrophoresis is considered the standard method for evaluation of protein concentrations as a result of its direct measurement, albumin is often quantified with biochemical assays. Many laboratory-based chemistry analyzers and clinic-based point-of-care analyzers use the dye bromocresol green (BCG) for the quantitation of albumin. Several studies have shown that albumin concentrations obtained by the standard (BCG) dye-binding method are significantly different from those obtained by protein electrophoresis in avian species and chelonia. The goal of this study was to compare plasma albumin concentrations obtained by the BCG method with those derived from electrophoresis in bearded dragons (Pogona vitticeps). Thirty-six heparinized plasma samples were obtained from 13 clinically healthy male bearded dragons. Albumin was quantified by protein electrophoresis and by the BCG dye-binding method. The two methods were significantly different (P < 0.0001, paired t-test; P < 0.0001, Wilcoxon signed-rank test), with the BCG measurement always equal to or higher than the electrophoretic result. The measurements from both methods were significantly correlated (r = 0.8634, P < 0.0001), but concordance between the two techniques was poor. The Bland-Altman plot appeared to show a greater difference between the two measurements with lower albumin values and lesser difference with higher values. These results indicate that bearded dragon plasma albumin concentration measurements obtained by the BCG dye-binding method are unreliable when compared to those obtained with electrophoresis, suggesting that albumin should be measured by protein electrophoresis for health assessment in bearded dragons.
Subject(s)
Blood Protein Electrophoresis/veterinary , Lizards/blood , Serum Albumin/analysis , Animals , Male , Serum Albumin/chemistryABSTRACT
Although serum protein electrophoresis is a diagnostic tool available through many veterinary laboratories, there currently are no reference intervals for protein fractions in healthy common mynahs (Acridotheres tristis). Therefore, electrophoretic patterns of proteins in serum and heparinized plasma of the common mynah were evaluated. Blood specimens were collected from 55 healthy adult common mynahs of unknown age (26 males and 29 females). The serum total protein and protein fractions were measured using the biuret method followed by cellulose acetate electrophoresis (CAE). The serum level of albumin was compared with bromocresol green (BCG) dye-binding and CAE methods. Four protein fractions, including albumin and α, ß, and γ globulins, were recorded in the electrophoretogram of serum specimens. Sex appeared to have no significant effect on the measured parameters. The serum BCG albumin fraction was significantly higher than the CAE albumin fraction (P = .01). Also, the comparison of total protein and protein fractions in serum and plasma specimens of 25 of the 55 birds sampled showed that total protein (Cohen index d = 0.66, P = .03), gamma globulin (d = 1.13, P = .00), and total globulin (d = 0.67, P = .00) in plasma samples were significantly higher than those in serum samples. The results of this study provide the specific reference intervals for total protein and protein fractions in common mynahs, which are essential for proper interpretation of laboratory results and also revealed that the albumin measurement by the BCG method yields unreliable results in common mynahs.
Subject(s)
Starlings , Animals , Blood Protein Electrophoresis/veterinary , Blood Proteins , Electrophoresis/veterinary , Electrophoresis, Cellulose Acetate/veterinary , Female , Male , Plasma , Serum AlbuminABSTRACT
Serum protein electrophoresis (EPH) is used to assess relative concentrations of blood proteins in clinical and biological studies. Serum EPH fractions have been determined for elasmobranchs using mammalian albumin, alpha 1-, alpha 2-, beta-, and gamma-globulin fractions, and have been deemed fractions 1 through 5, respectively. However, serum EPH fraction concentration reference intervals (RIs) have not been widely established for different elasmobranch species. In this study, RIs for fractions 1 through 5 were determined from 45 wild-caught Nurse Sharks Ginglymostoma cirratum (27 females and 23 males) in South Florida. Serum samples were isolated from whole blood following caudal venipuncture. Body condition was also measured in the field to assess the relative health of the individuals sampled. There was no relationship between body condition and serum EPH fraction concentrations. In addition, there was no difference in body condition or serum EPH fraction concentrations between females and males. Total solids and total protein values were significantly different (P < 0.001). Nurse Shark serum EPH fraction 1 was found within the mammalian albumin migrating band distance and was negligible. Fraction 2 showed no peak in the mammalian alpha 1-globulin range. A thin, medium peak in the mammalian alpha 2-globulin range represented fraction 3. In the mammalian beta-globulin range, fraction 4 consisted of the majority of protein observed. It was represented by a smooth, broad peak. A short, medium broad peak in the mammalian gamma-globulin range represented fraction 5. The Nurse Shark serum EPH fraction RIs provided in this study may be utilized to clinically evaluate the health of Nurse Sharks in captivity and in the wild, and to compare the health of their populations around the world experiencing various anthropogenic stressors and other environmental impacts.
Subject(s)
Blood Protein Electrophoresis/veterinary , Blood Proteins/analysis , Sharks/blood , Animals , Female , Florida , Male , Reference ValuesABSTRACT
There are no published plasma biochemistry reference intervals for any species within the order Gaviiformes, which includes the common loon (Gavia immer). Because of their unique classification and lack of close taxonomic relatives, species-specific values for clinical data in loons are needed. This study determined reference intervals for plasma biochemical values in adult common loons, and reference intervals for protein electrophoresis values in both adult and juvenile common loons. Healthy, wild adult (n = 148, age >3 yr) and juvenile (n = 31, age 4-12 wk) common loons were sampled on freshwater summer breeding territories at study sites across North America. Plasma biochemical analytes included glucose (Glu), total calcium, phosphorus, sodium, potassium, chloride, blood urea nitrogen (BUN), uric acid, cholesterol, triglycerides, creatine kinase, γ-glutamyl transferase, alkaline phosphatase (ALP), lactate dehydrogenase, aspartate aminotransferase, amylase, and bile acids. Protein electrophoresis data included albumin to globulin ratio (A: G), prealbumin, albumin, α1-globulin, α2-globulin, ß-globulin, and γ-globulin. Adult females had significantly higher Glu, ALP, and BUN than adult males. Juvenile loons had higher ß-globulins than adults, whereas adults had higher α1-globulins. Establishment of complete reference intervals will improve clinical assessment of captive loons, and allow researchers to better understand the health of wild loons in response to the multiple environmental stressors faced by these species.
Subject(s)
Birds/blood , Blood Chemical Analysis/veterinary , Blood Protein Electrophoresis/veterinary , Plasma/chemistry , Animals , Female , Male , Reference ValuesABSTRACT
Pronghorn (Antilocapra americana) are native to western North America and are found in 24 Association of Zoos and Aquariums (AZA)-accredited institutions. Acute-phase proteins (APP) are a broad class of proteins that are stimulated in response to inflammation and have been shown to be a sensitive measure of inflammation in equids and ruminants. In this study, blood samples from clinically normal free-ranging and captive populations of pronghorn were analyzed using assays for protein electrophoresis (EPH) and APP, including serum amyloid A (SAA) and haptoglobin (HP), to develop preliminary ranges to gauge potential differences between these populations. Additional samples were taken from clinically abnormal captive pronghorn with facial abscesses. By EPH measurements, albumin: globulin ratio mean and SE were significantly different (P <0.05) with 1.02 (0.08) for captive populations and 1.91 (0.05) for free-ranging populations. Total protein mean and SE were significantly different (P <0.05) for captive and free-ranging populations, respectively 5.6 (0.3) g/dl and 6.9 (0.1) g/dl. Mean and SD of SAA for captive pronghorn were 1.4 (3.2) mg/L, and were significantly different from the free-ranging population, which was below the limits of detection for (P <0.05). There was no difference in HP levels between these groups. In a case study of a pronghorn with facial abscesses, elevated levels of HP, but not SAA, suggested that HP maybe useful in certain disease states. Future studies should explore the use of these biomarkers as tools to monitor general health, prognosis, and subclinical disease.
Subject(s)
Acute-Phase Proteins/metabolism , Animals, Wild/blood , Animals, Zoo/blood , Blood Protein Electrophoresis/veterinary , Ruminants/blood , Animals , Female , Male , North America , Reference Values , TexasABSTRACT
Agarose gel electrophoresis (AGE) has been widely implemented throughout veterinary medicine and for analysis of plasma proteins of avian and reptile species. Capillary zone electrophoresis (CZE) is becoming a standard method in human clinical pathology laboratories but has not widely been used for the analysis of animal samples. The objective of the present study was to compare protein fractions derived from AGE and CZE methods using plasma from the green turtle (Chelonia mydas). Plasma samples were analyzed by AGE and CZE per manufacturer guidelines. The methods were assessed by CV analysis, Spearman's correlation, Passing-Bablok regression, and Bland Altman plots. CZE consistently resolved more fractions than AGE with three fractions observed in the prealbumin migrating region versus one for AGE and two fractions in the γ globulin region versus one for AGE. Compared with AGE, CZE showed a lower CV in intra-assay tests (1.0-4.9% vs 2.0-28.3%) and a lower or overlapping CV in interassay tests (1.0-10.6 vs 2.3-22.0). The prealbumin, α2 globulin, and ß globulin fractions correlated the least between the methods (for all three fractions: rs ≤ 0.28, P > 0.21). Moderate, significant correlations between AGE and CZE methods were observed for albumin (rs = 0.78, P < 0.0001) and γ globulins (rs = 0.78, P < 0.0001). CZE has a higher precision and ease of use over AGE and offers the opportunity to resolve additional protein fractions. This will necessitate the development of new conventions in placement of fraction delimits, definition of species-specific reference intervals, and evaluation of clinical utility in abnormal turtles.
Subject(s)
Blood Protein Electrophoresis/veterinary , Electrophoresis, Agar Gel/veterinary , Electrophoresis, Capillary/veterinary , Plasma/chemistry , Turtles/blood , Animals , Blood Protein Electrophoresis/methods , Blood Proteins/analysis , Electrophoresis, Agar Gel/methods , Electrophoresis, Capillary/methods , Species SpecificityABSTRACT
Acute-phase proteins (APP) are the foundation to the innate immune response and valuable biomarkers that increase with inflammation, infection, neoplasia, stress, and trauma.2,4,16 Little is known about the acute-phase response in cetaceans and if these proteins can be used for health monitoring in individuals and free-ranging populations. The purpose of this study was to characterize serum concentrations of haptoglobin (Hp) and serum amyloid A (SAA), as well as electrophoretic profiles of common bottlenose dolphins (Tursiops truncatus) in free-ranging (n = 33) and professional care (n = 27) settings. Results were correlated to commonly utilized inflammatory indices including erythrocyte sedimentation rate (ESR), fibrinogen, total white blood cell count (WBC), and absolute neutrophil count. SAA levels, measured with a dolphin-specific enzyme linked immunosorbent assay (ELISA), were significantly higher (P = 0.05) in free-ranging dolphins (mean = 4.26; SE = 1.12) when compared with those under professional care (mean = 1.82; SE = 0.45). For dolphins under professional care, a statistically significant correlation was identified between ESR and Hp (P < 0.001; r = 0.69), ESR and SAA (P < 0.001; r = 0.67), fibrinogen and Hp (P = 0.001; r = 0.58), and fibrinogen and SAA (P = 0.002; r = 0.56). In addition, there was a significant correlation between WBC and SAA (P = 0.01; r = 0.38) and absolute neutrophil count and SAA (P = 0.04; r = 0.32). There were no significant correlations between study variables observed in free-ranging dolphins. The variable correlation of APPs with commonly utilized inflammatory indices demonstrates that these proteins are independent measures of inflammation with unique sensitivity, specificity, and timeline of expression. The results of this study contribute to improved health monitoring of dolphins and have the potential to assist in identification of compromised health.
Subject(s)
Blood Sedimentation , Bottle-Nosed Dolphin/blood , Fibrinogen/metabolism , Haptoglobins/metabolism , Leukocyte Count/veterinary , Serum Amyloid A Protein/metabolism , Animals , Blood Protein Electrophoresis/veterinary , Female , Florida , Male , Serum/chemistryABSTRACT
BACKGROUND: Capillary electrophoresis of plasma proteins has shown great potential as a complementary diagnostic tool for avian species. However, reference intervals for plasma proteins are sparse or lacking for several free-living avian species. The current study reports electrophoretic patterns and concentrations of plasma proteins determined for 70 free-living white-tailed eagle (Haliaeetus albicilla) nestlings from two locations in Norway (Steigen and Smøla) in order to establish reference values for this subpopulation using capillary electrophoresis. The nestlings were between 44 and 87 days of age, and the plasma protein concentrations were investigated for age, sex, year (2015 and 2016) and location differences. To our knowledge, this is the first report of reference intervals of plasma proteins analysed by capillary electrophoresis in free-living white-tailed eagle nestlings. RESULTS: The plasma protein concentrations (% of total protein, mean ± SE) were determined for prealbumin (13.7%, 4.34 ± 0.15 g/L), albumin (46.7%, 14.81 ± 0.24 g/L), α1-globulin (2.4%, 0.74 ± 0.03 g/L), α2-globulin (11.7%, 3.72 ± 0.06 g/L), ß-globulin (15.9%, 5.06 ± 0.08 g/L) and γ-globulin (9.6%, 3.05 ± 0.09 g/L). Significant differences were found between the two locations for prealbumin, α2- and γ-globulins. No significant differences were found between the two sampling years or sexes, and no effect of age was found for any of the plasma proteins. However, prealbumin levels were several folds higher than previously reported from adults of closely related birds of prey species. There were no other studies on capillary electrophoresis of nestling plasma available for comparison. CONCLUSION: Significant differences were found between sampling locations for prealbumin, α2- and γ-globulins, which may indicate differences in inflammatory or infectious status between nestlings at the two locations. Sampling year, sex or age had no significant effect on the plasma protein concentrations. These results provide novel data on plasma protein concentrations by capillary electrophoresis and may be useful for evaluation of health status in free-living white-tailed eagle nestlings.
Subject(s)
Blood Protein Electrophoresis/veterinary , Blood Proteins/chemistry , Eagles/blood , Animals , Female , Male , NorwayABSTRACT
Parturition is one of the most important events in reproduction. Regardless of many studies, exact time for pregnancy termination and onset of parturition is impossible to determine. The aim of this study was to describe and to compare protein profile of plasma from healthy pregnant cows (n = 6) at following five time points: 2 weeks, 1 week before, at parturition, 1 week and 2 weeks after parturition to search for possible protein markers of parturition. Plasma samples were analysed by 1D and 2D electrophoresis, and selected spots were identified by mass spectrometry. Protein profile showed no uniform pattern. Seventy spots differed at least for one sampling point from the time point 2 weeks before parturition which served as reference. Thirty spots expressed higher intensity of staining 1 week as 2 weeks before parturition while 13 showed opposite relationship. Twenty two spots expressed higher intensity of staining at parturition as 2 weeks before delivery while 15 showed opposite relationship. Eighteen spots expressed higher intensity of staining 2 weeks before parturition as 1 week post-partum while 2 showed opposite relationship. Fifteen spots expressed higher intensity of staining 2 weeks before parturition as 2 weeks after delivery while 14 showed opposite relationship. Thirty-five proteins, belonging to different functional groups, were identified. Of them, 15 spots differed significantly between parturition and 2 weeks before delivery. Among them were metalloproteinase inhibitor and LDH which seem to be the most promising molecules considered as parturition markers due to their functions.
Subject(s)
Biomarkers , Blood Proteins/metabolism , Cattle/physiology , Parturition/blood , Animals , Blood Protein Electrophoresis/veterinary , Female , Mass Spectrometry , PregnancyABSTRACT
A 15-yr-old cockatiel (Nymphicus hollandicus) presented with decreased activity and appetite. A presumptive diagnosis of lymphoproliferative disease was made because of a monoclonal band observed on plasma protein electrophoresis. The owner declined further diagnostics or treatment, and the bird died 2 yr later. In a second case, a 4-yr-old blue and gold macaw (Ara ararauna) presented with lethargy and anorexia. Despite supportive treatment, the bird died 7 days later. Blood studies also demonstrated a monoclonal band on plasma protein electrophoresis. The histologic review of tissues from both birds found extensive neoplastic lymphoplasmocytic cells in the liver and supported a diagnosis of lymphosarcoma.
Subject(s)
Bird Diseases/diagnosis , Blood Protein Electrophoresis/methods , Lymphoma, Non-Hodgkin/veterinary , Parrots , Animals , Bird Diseases/therapy , Blood Protein Electrophoresis/veterinary , Fatal Outcome , Hypergammaglobulinemia/diagnosis , Hypergammaglobulinemia/therapy , Hypergammaglobulinemia/veterinary , Liver/pathology , Lymphoma, Non-Hodgkin/diagnosis , Lymphoma, Non-Hodgkin/therapy , MaleABSTRACT
Grant's zebra (Equus burchelli) are commonly kept in zoos and are subject to routine health monitoring and research studies. Recently, assays for acute phase proteins (APP) have been described in many wildlife species, and specific assays for serum amyloid A (SAA) have been well validated and studied in horses (Equus ferus caballus), in which it serves as a major APP. In the present study, serum samples from 26 Grant's zebra were subject to analysis by using assays for SAA, haptoglobin (HP), and protein electrophoresis. Reference intervals were calculated by using the robust method: SAA 1.8-31.4 mg/L and HP 0.37-1.58 mg/ml. Significant differences in SAA and HP were observed in clinically abnormal zebra; in some cases, these differences were marked and were noted in the absence of abnormal values for protein electrophoretic fractions. These data indicate that APP may be a valuable and sensitive tool in monitoring inflammation in this species.
Subject(s)
Acute-Phase Proteins/metabolism , Blood Protein Electrophoresis/veterinary , Blood Proteins/metabolism , Equidae/blood , Animals , Biomarkers , Equidae/classification , Reference ValuesABSTRACT
Elegant-crested tinamou (Eudromia elegans) are members of the family Tinamidae. A review of postmortem records at the Saint Louis Zoo suggests that this species is highly susceptible to aspergillosis. Antemortem detection of Aspergillus infections can be aided by evaluating results of hematologic, plasma biochemical, protein electrophoretic, and Aspergillus antigen and antibody serologic testing. To establish species-specific reference intervals for these parameters in elegant-crested tinamou, blood samples were collected and analyzed from 19 healthy captive adult and subadult elegant-crested tinamou. The predominant circulating leukocyte in elegant-crested tinamou is the lymphocyte. Prealbumin electrophoresis fractions were detected in 4 of 19 birds (21%), and globulin fractions were detected in all birds. All birds had measurable titers for Aspergillus antibody and galactomannan antigen, including 3 birds with antibody levels considered to be positive. Galactomannan levels were all below the positive threshold of 1.0. Results of hematologic and plasma biochemical analyses performed on blood samples obtained from terminally ill elegant-crested tinamou with confirmed aspergillosis were compared with results from healthy individuals. Significant differences were found in the hematocrit, total white blood cell count, heterophil and monocyte counts, and albumin and globulin levels.
Subject(s)
Aspergillus/isolation & purification , Birds/blood , Blood Chemical Analysis/veterinary , Blood Protein Electrophoresis/veterinary , Animals , Blood Chemical Analysis/standards , Female , Male , Reference ValuesABSTRACT
BACKGROUND: Densitometric quantification of myeloma paraproteins (M-proteins) is used to monitor secretory myeloma related disorders in humans and dogs. The previous work in dogs used agarose gel electrophoresis (AGE) but did not establish if other methods of serum protein electrophoresis, such as capillary zone electrophoresis (CZE), were comparable. OBJECTIVES: We aimed to determine if the densitometric quantification of M-proteins using CZE would yield results comparable to AGE methods. METHODS: Fifty-one serum samples from 22 dogs and 18 cats with confirmed monoclonal gammopathies and previously performed AGE were evaluated using CZE on a Sebia Minicap system. Samples were run in duplicate, and their M-proteins were densitometrically measured using the corrected perpendicular drop method previously described. Human-based quality control samples were used to determine the inter-run coefficient of variation (CV). Patient samples were used to calculate the intra-run CV. Method comparison was performed using simple linear regression, Passing-Bablok regression, and Bland-Altman analyses, and Medx evaluations. RESULTS: Inter-run and intra-run CVs for CZE were 3.71%-7.65% and 2.89%-4.74%, respectively. Simple linear regression demonstrated an excellent correlation (r > 0.98). Passing-Bablok regression was compatible with the presence of proportional bias in the entire population, and Bland-Altman plots revealed a proportional bias in the feline cases. The Medx evaluation suggested that the two methods did not perform similarly in clinical samples with poor performance at a decision limit of 0.5 gm/dL. CONCLUSIONS: Capillary zone electrophoresis is an acceptable method for M-protein densitometric quantification in canine and feline sera but cannot be used interchangeably with AGE-based evaluations.
Subject(s)
Cat Diseases , Dog Diseases , Animals , Blood Protein Electrophoresis/veterinary , Cats , Dog Diseases/diagnosis , Dogs , Electrophoresis, Agar Gel/veterinary , Electrophoresis, Capillary/veterinary , HumansABSTRACT
BACKGROUND: The diagnostic performance of routine electrophoresis (agarose gel electrophoresis [AGE] and capillary zone electrophoresis [CZE]) and species-specific immunofixation (IF) for the detection of immunoglobulin paraproteins (M-proteins) and diagnosis of secretory myeloma-related disorders (sMRD) can be improved. Available canine IF targets were IgG-FC, IgA, IgM, light chain (LC), IgG4, and free LC (fLC) antibodies. OBJECTIVE: We aimed to review specific features associated with the presence of M-proteins in canine serum samples and the common features causing inaccurate reporting of M-proteins to improve the diagnostic performance of routine electrophoresis and IF for the detection of M-proteins. METHODS: Features found in AGE, CZE, routine IF, IgG4 IF, and fLC IF of 100 canine serum samples from Part 1 of this study were evaluated by simple and multivariate logistic regression to identify factors associated with the presence of M-proteins. Cases falsely called negative or positive for M-proteins were reviewed to identify the common features that could be used to increase the diagnostic performance of SPE and IF for M-protein detection. RESULTS: The presence of hypogammaglobulinemia or any peak taller than albumin was associated with an M-protein. Total protein concentrations, globulin concentrations, or peaks wider than albumin were not associated with an M-protein. Free LC sMRD cases were not diagnosed by SPE and routine IF. Cases with infectious and inflammatory etiologies had a restricted polyclonal gammopathy with multiple γ-globulin restrictions resulting in some false-positive results. SPE combined with all available IF results and the specific features identified in this study had an estimated sensitivity of 95.1% and specificity of 81.4%. CONCLUSIONS: The identified criteria of this study increase the diagnostic performance of the electrophoretic evaluation for M-proteins.
Subject(s)
Dog Diseases , Multiple Myeloma , Animals , Blood Protein Electrophoresis/veterinary , Dogs , Immunoelectrophoresis/veterinary , Immunoglobulin Light Chains , Multiple Myeloma/veterinary , ParaproteinsABSTRACT
Beta-gamma bridging (ß-γ bridging) on serum protein electrophoresis is touted as being virtually pathognomonic for hepatic disease. However, the criteria for ß-γ bridging are not defined, and few publications support a relationship between ß-γ bridging and liver disease. The goal of this retrospective study was to evaluate the prevalence of hepatic pathology in animals with ß-γ bridging. All serum protein electrophoretograms from clinical patients generated at the University of Georgia between 1994 and 2008 were evaluated for the presence of ß-γ bridging, defined as (1) an albumin:globulin ratio below the reference interval; (2) indistinct separation between all ß and γ globulin fractions or between the ß(2) and γ fractions, with a negative shoulder slope of < 5%; and (3) predominance of γ proteins versus ß proteins. Of the 237 electrophoretograms examined, 25 (11 dogs, 11 cats, 3 horses) met the inclusion criteria for ß-γ bridging. Patients were classified into disease categories on the basis of biochemical, cytologic, and/or histologic findings. Positive predictive values of ß-γ bridging for hepatic and infectious diseases were determined with a one-sided exact binomial test. Of 25 animals, 8 had evidence for hepatic disease, whereas 9 had infectious diseases. As such, the positive predictive value of ß-γ bridging for hepatic disease was 32.0%, with a 95% confidence interval of 15.0% to 53.5% (P < .001), whereas for infectious disease, the positive predictive value was 36.0%, with a similar confidence interval. Beta-gamma bridging is not pathognomonic for liver diseases and is as frequently found with infectious diseases.
Subject(s)
Beta-Globulins/analysis , Blood Protein Electrophoresis/veterinary , Cat Diseases/diagnosis , Dog Diseases/diagnosis , Horse Diseases/diagnosis , Liver Diseases/veterinary , gamma-Globulins/analysis , Animals , Cat Diseases/blood , Cats , Dog Diseases/blood , Dogs , Horse Diseases/blood , Horses , Liver Diseases/blood , Liver Diseases/diagnosis , Predictive Value of Tests , Sensitivity and SpecificityABSTRACT
OBJECTIVE: To determine reference intervals for concentrations of plasma total protein (TP) and electrophoretogram fractions (ELFs) for healthy, wild loggerhead sea turtles (Caretta caretta) and green turtles (Chelonia mydas) and to assess relationships between TP and ELF concentrations and health status, body size, body mass, and water temperature. DESIGN: Evaluation study. ANIMALS: 437 healthy and 35 ill Atlantic loggerhead sea turtles and 152 healthy and 3 ill Atlantic green turtles. PROCEDURES: Free-ranging turtles were captured from a nuclear power plant intake canal in southern Florida. Plasma samples were obtained from all turtles. Plasma TP and ELF concentrations were measured, and reference intervals were calculated. Wilcoxon rank-sum tests were used to compare TP and ELF values between healthy and ill loggerhead sea turtles. Spearman rank correlations were evaluated between concentrations of TP and ELFs and carapace length, body mass, and water temperature. RESULTS: Reference intervals for TP concentrations were 2.2 to 5.2 g/dL and 2.0 to 5.4 g/dL for loggerhead sea turtles and green turtles, respectively. Except for gamma-globulin, concentrations of ELFs were significantly higher in healthy than in ill loggerhead sea turtles. There was a positive correlation between TP, alpha-globulin, beta-globulin, and gamma-globulin concentrations and water temperature in loggerhead sea turtles and between only TP and alpha-globulin concentrations and water temperature in green turtles. CONCLUSIONS AND CLINICAL RELEVANCE: Reference intervals for concentrations of TP and ELFs for healthy, free-ranging loggerhead sea turtles and green turtles can be used in combination with other diagnostic tools to assess health status of sea turtles.
Subject(s)
Blood Protein Electrophoresis/veterinary , Blood Proteins/chemistry , Body Size/physiology , Turtles/anatomy & histology , Turtles/physiology , Animal Diseases/blood , Animals , Ecosystem , Reference Values , Seawater , Species Specificity , Temperature , Turtles/bloodABSTRACT
Blood samples were collected from captive, adult, clinically normal Indian peafowl (Pavo cristatus) for hematologic and plasma biochemical analyses. Hematologic parameters investigated were total red blood cell count, hemoglobin, packed cell volume, fibrinogen, mean cell volume, mean cell hemoglobin, mean cell hemoglobin concentration, total white blood cell count, differential white blood cell count, and thrombocyte count. Plasma biochemical parameters investigated were alanine aminotransferase, alkaline phosphatase, amylase, aspartate aminotransferase, bile acids, total bilirubin, blood urea nitrogen, calcium, cholesterol, creatinine, creatine kinase, gamma glutamyltransferase, lactate dehydrogenase, glucose, iron, phosphorus, and uric acid, as well as plasma protein electrophoresis. Results were compared with values from studies done in houbara bustards (Chlamydotis undulata), kori bustards (Ardeotis kori), stone curlews (Burhinus oedicnemus), and taxonomically related species, including ring-necked pheasants (Phasianus colchicus), red-legged partridges (Alectoris rufa), Kashmir native fowl (Kashmirfavorella), and Bangladesh native, Fayoumi, and Assil fowl (Gallus domesticus).
Subject(s)
Blood Chemical Analysis/veterinary , Galliformes/blood , Animals , Blood Protein Electrophoresis/veterinary , Female , Hematologic Tests/veterinary , Male , Reference ValuesABSTRACT
Veterinarians rely on results of both the complete blood cell count (CBC) and plasma protein electrophoresis (EPH) in conjunction with the results of the plasma biochemical analysis to evaluate the health status of avian patients. Because the CBC and protein EPH measure different aspects of the immune response to disease, both tests are recommended in avian patients to rule out infectious or inflammatory disease. To evaluate results of the CBC and protein EPH in pet psittacine birds, the records of 144 pet psittacine birds, comprising 11 genera, that were presented for suspected illness were reviewed. Results of the CBC (total white blood cell count and packed cell volume) and protein EPH (alpha, beta, and gamma globulin concentrations) from submitted blood samples from each bird were evaluated. Of the 144 birds, 63 (43.8%) had abnormal CBC results, and 25 (17.4%) had abnormal EPH measurements. Results of the CBC and protein EPH were within reference ranges in 73 birds (50.7%). Abnormal results of the CBC in conjunction with normal EPH results were present in 46 birds (31.9%), compared with 8 birds (5.6%) with normal results of the CBC and abnormal EPH results. The findings of this study could aid practitioners in evaluating psittacine patients and prioritizing the value of individual diagnostic tests.