ABSTRACT
Disease of the kidney developed in breeding stock of Gunn rats. The renal lesion is the result of a new mutation. The genetic defect is inherited as an autosomal dominant trait and is apparently lethal in the homozygous condition. The abnormality manifests itself as a congenital hydronephrosis with related cystic changes in the kidney.
Subject(s)
Hydronephrosis/congenital , Kidney Diseases, Cystic/genetics , Kidney Diseases/genetics , Mutation , Rats , Rodent Diseases , Animals , Genes, Dominant , Heterozygote , Homozygote , Hydronephrosis/pathology , Jaundice/genetics , Kidney Diseases, Cystic/pathology , Models, Biological , UrographyABSTRACT
Hemoglobin from an adult camel (Camelus dromedarius) was prepared from the red cell lysate by CM- and DEAE-cellulose chromatography. The purified hemoglobin showed a lesser mobility on starch gel electrophoresis at pH 8.5 than that of human hemoglobin C. Native camel hemoglobin contains 95-99% alkali-resistant hemoglobin and in soluble in 2.94 M K2HPO4/KH2PO4 buffer. Different forms of camel hemoglobin show similar ammonium sulfate precipitation curves. Indirect evidence for the stability of camel hemoglobin solutions was obtained from several sources. Spontaneous met-hemoglobin formation is extremely slow and minimal quantities of degradation products appear on starch gel electrophoresis and on chromatographic separation. The alpha and beta chains of camel hemoglobin A were separated on a CM-23 column by the use of a pyridine formate gradient. Large peptide fragments were obtained by tryptic digestion of maleylated alpha and beta chains. The N-terminal structure of the alpha and beta chains and of tryptic maleylated peptides derived from alpha and beta chains are presented. Between adult camel hemoglobin and adult human hemoglobin six amino acid differences in the N-terminal 20 amino acid residues of the alpha chain, at residues: 4, 5, 12, 14, 17, and 19; eight amino acid substitutions were found in the beta chain at positions: 4, 5, 6, 9, 12, 13, 16, and 19. Substitutions at alpha5 Ala leads to Lys, and beta19 Asn leads to Lys, increase the net positive charge of camel hemoglobin by two, while other substitutions result in no charge differences. The molecular basis of the stability of camel adult hemoglobin is discussed.
Subject(s)
Camelus/blood , Hemoglobins , Amino Acid Sequence , Animals , Binding Sites , Blood Protein Electrophoresis , Electrophoresis, Starch Gel , Humans , Hydrogen-Ion Concentration , Macromolecular Substances , Maleates , Oxyhemoglobins , Peptide Fragments/analysis , Protein Binding , Protein Denaturation , TrypsinSubject(s)
Animals, Laboratory , Costs and Cost Analysis , Equipment and Supplies/veterinary , Veterinary Medicine , Animals , Cat Diseases/diagnosis , Cats , Cricetinae , Dog Diseases/diagnosis , Dogs , Ectromelia/diagnosis , Ectromelia/veterinary , Feces/microbiology , Mice , Monitoring, Physiologic , Parasitic Diseases/diagnosis , Parasitic Diseases, Animal , Pseudomonas Infections/diagnosis , Pseudomonas Infections/veterinary , Rabbits , Rats , Research , Rodent Diseases/diagnosis , Salmonella Infections/diagnosis , Salmonella Infections, AnimalABSTRACT
The primary structure of adult marmoset hemoglobin has been determined. The alpha- and beta-chains of HbA were separated on a CM23 column in 8 M urea using a sodium phosphate gradient. Tryptic digest of the alpha- and beta-chains were fractionated on a Dowex 50W-X2 column using a pH and pyridine acetate gradient. Large peptide fragments were obtained by the cyanogen bromide cleavage of the alpha- and beta-chains, as well as by tryptic digestion of the maleylated alpha- and beta-chains. The sequence was derived from the amino acid compositions and sequences of the individual tryptic peptide, automated sequence determination of intact alpha- and beta-chains, as well as automated sequence determination of cyanogen bromide fragments and tryptic maleylated peptides derived from the alpha- and beta-chains. The complete structure of marmoset adult hemoglobin is closely homologous to that of other primate hemoglobins. The sequence of the marmoset alpha-chain differs from the alpha-chian of human HbA at positions 8, 19, 23, 68, and 116. The beta-chain from marmoset HbA differs from the beta-chain of human HbA at positions 5, 13, 21, 50, 87, and 125.
Subject(s)
Callitrichinae/blood , Hemoglobins , Amino Acid Sequence , Amino Acids/analysis , Animals , Haplorhini , Humans , Macromolecular Substances , Maleates , Peptide Fragments/analysis , Species Specificity , TrypsinABSTRACT
The Transfusion Safety Study (TSS) and the National Heart, Lung, and Blood Institute (NHLBI) established a repository of approximately 200,000 sera from blood donors in late 1984 and early 1985. Collections were made in the four metropolitan areas with the highest prevalence of AIDS. Retrospective testing showed an overall anti-HIV-1 prevalence of 16 cases per 10,000 donations. In this study, the predictive value of a negative initial enzyme-linked immunoassay was estimated from both quality control specimens and the rescreening of 13,461 sera to be greater than 99.99 percent with respect to technical error. Among anti-HIV-1-positive persons, there was a 1.3- to 1.5-fold excess of first-time donors. The anti-HIV-1 prevalence among donors showed that infection was more common among young men than suggested by national reporting of AIDS cases. Anti-HIV-1 prevalence varied among the four metropolitan areas less than did reported AIDS cases, but, by 1987, the differences in the latter had decreased. Anti-HIV-1 prevalence in collection areas outside of the four major cities differed much more widely than that among the cities themselves. The TSS/NHLBI Donor Repository will remain available for the indefinite future for further evaluation of screening procedures for HIV-1 and other viruses for which transfusion is found to be an important route of transmission.