RESUMO
OBJECTIVES: The Government of India prohibited the sale of tobacco products during the COVID-19 lockdown to prevent the spread of the SARS-CoV-2 virus. This study assessed the tobacco cessation behaviour and its predictors among adult tobacco users during the initial COVID-19 lockdown period in India. METHODS: A cross-sectional study was conducted with 801 adult tobacco users (both smoking and smokeless tobacco) in two urban metropolitan cities of India over a 2-month period (July to August 2020). The study assessed complete tobacco cessation and quit attempts during the lockdown period. Logistic and negative binomial regression models were used to study the correlates of tobacco cessation and quit attempts, respectively. RESULTS: In total, 90 (11.3%) tobacco users reported that they had quit using tobacco after the COVID-19 lockdown period. Overall, a median of two quit attempts (interquartile range 0-6) was made by tobacco users. Participants with good knowledge on the harmful effects of tobacco use and COVID-19 were significantly more likely to quit tobacco use (odds ratio [OR] 2.2; 95% confidence interval [CI] 1.2-4.0) and reported more quit attempts (incidence risk ratio 5.7; 95% CI 2.8-11.8) compared to those with poor knowledge. Participants who had access to tobacco products were less likely to quit tobacco use compared to those who had no access (OR 0.3; 95% CI 0.2-0.5]. CONCLUSIONS: Access restrictions and correct knowledge on the harmful effects of tobacco use and COVID-19 can play an important role in creating a conducive environment for tobacco cessation among users.
Assuntos
COVID-19 , Abandono do Hábito de Fumar , Abandono do Uso de Tabaco , Adulto , Controle de Doenças Transmissíveis , Estudos Transversais , Humanos , Índia , SARS-CoV-2RESUMO
BACKGROUND AND OBJECTIVES: Positive samples identified during routine serological screening for HCV (hepatitis C virus), HBV (hepatitis B virus) and HIV (human immunodeficiency virus) are confirmed by nucleic acid testing in the SNBTS (Scottish National Blood Transfusion Service) PCR Reference laboratory. Serological screening for HTLV-I (human T-cell lymphotropic virus type I) and -II was implemented in Scotland in November 2002, at which time a PCR assay was not available for confirmation. Our aim was to develop a real-time PCR assay that could be used for the confirmation of samples showing HTLV-I serological positive or indeterminate reactivity and to investigate whether a serologically silent carrier status exists ('Tax' only) in the Scottish donor population. MATERIALS AND METHODS: A real-time HTLV PCR was devised using a lymphoblastoid cell line which has HTLV-I sequence integrated in the genome (C8166 cells). These were spiked into peripheral blood mononuclear cells. The assay was evaluated on archived serologically confirmed HTLV-positive samples and new positives identified since implementation of screening. RESULTS: HTLV-I and -II were detected in cells and plasma from stored donations and a serological positive donation identified in routine screening. HTLV DNA can also be amplified from the plasma obtained from plasma preparation tubes. There was no evidence of a carrier status ('Tax' only) in 100 serologically negative blood donors tested. The PCR assay developed is reliable and sensitive, capable of identifying one copy of HTLV-I. CONCLUSIONS: The HTLV PCR is a useful addition for HTLV confirmation, especially in serologically indeterminate samples and for look-back studies. HTLV PCR confirmation will provide additional useful information for donor medical staff for counselling donors.
Assuntos
Doadores de Sangue , Transfusão de Sangue , Vírus Linfotrópico T Tipo 1 Humano/genética , Vírus Linfotrópico T Tipo 2 Humano/genética , Reação em Cadeia da Polimerase/métodos , Genes pX/genética , Infecções por HTLV-I/diagnóstico , Infecções por HTLV-II/diagnóstico , Vírus Linfotrópico T Tipo 1 Humano/imunologia , Vírus Linfotrópico T Tipo 2 Humano/imunologia , Humanos , Programas de Rastreamento/métodos , Escócia , Testes Sorológicos/métodosRESUMO
We have studied the evolution of hepatitis C virus (HCV) from a common source following serial transmission from contaminated batches of anti-D immunoglobulin. Six secondary recipients were each infected with virus from identifiable primary recipients of HCV-contaminated anti-D immunoglobulin. Phylogenetic analysis of virus E1/E2 gene sequences [including the hypervariable region (HVR)] and part of NS5B confirmed their common origin, but failed to reproduce the known epidemiological relationships between pairs of viruses, probably because of the frequent occurrence of convergent substitutions at both synonymous and nonsynonymous sites. There was no evidence that the rate at which the HCV genome evolves is affected by transmission events. Three different mechanisms appear to have been involved in generating variation of the hypervariable region; nucleotide substitution, insertion/deletion of nucleotide triplets at the E1/E2 boundary and insertion of a duplicated segment replacing almost the entire HVR. These observations have important implications for the phylogenetic analysis of HCV sequences from epidemiologically linked isolates.
Assuntos
Evolução Molecular , Variação Genética , Genoma Viral , Hepacivirus/genética , Hepatite C/transmissão , Adolescente , Adulto , Idoso , Sequência de Aminoácidos , Sequência de Bases , Transfusão de Sangue , Criança , Contaminação de Medicamentos , Feminino , Hepatite C/epidemiologia , Hepatite C/virologia , Humanos , Transmissão Vertical de Doenças Infecciosas , Irlanda/epidemiologia , Masculino , Dados de Sequência Molecular , Mutação/genética , Filogenia , Estudos Retrospectivos , Imunoglobulina rho(D)/administração & dosagem , Proteínas do Envelope Viral/química , Proteínas do Envelope Viral/genéticaRESUMO
The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin. Misfolding in rhodopsin, characterized by the loss of ability to bind 11-cis-retinal, has been shown to be caused by an intradiscal disulfide bond different from the above native disulfide bond. Further, naturally occurring single mutations of the intradiscal cysteines (C110F, C110Y, and C187Y) are associated with retinitis pigmentosa (RP). To elucidate further the role of every one of the three intradiscal cysteines, mutants containing single-cysteine replacements by alanine residues and the above three RP mutants have been studied. We find that C110A, C110F, and C110Y all form a disulfide bond between C185 and C187 and cause loss of retinal binding. C185A allows the formation of a C110-C187 disulfide bond, with wild-type-like rhodopsin phenotype. C187A forms a disulfide bond between C110 and C185 and binds retinal, and the pigment formed has markedly altered bleaching behavior. However, the opsin from the RP mutant C187Y forms no rhodopsin chromophore.
Assuntos
Cisteína , Dobramento de Proteína , Estrutura Secundária de Proteína , Rodopsina/química , Rodopsina/metabolismo , Sequência de Aminoácidos , Substituição de Aminoácidos , Animais , Bovinos , Humanos , Dados de Sequência Molecular , Mutagênese Sítio-Dirigida , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Retinose Pigmentar/genética , Rodopsina/genética , Opsinas de Bastonetes/química , Opsinas de Bastonetes/genética , Opsinas de Bastonetes/metabolismo , EspectrofotometriaRESUMO
The long-term evolution of the hepatitis C virus hypervariable region (HVR) and flanking regions of the E1 and E2 envelope proteins have been studied in a cohort of women infected from a common source of anti-D immunoglobulin. Whereas virus sequences in the infectious source were relatively homogeneous, distinct HVR variants were observed in each anti-D recipient, indicating that this region can evolve in multiple directions from the same point. Where HVR variants with dissimilar sequences were present in a single individual, the frequency of synonymous substitution in the flanking regions suggested that the lineages diverged more than a decade previously. Even where a single major HVR variant was present in an infected individual, this lineage was usually several years old. Multiple lineages can therefore coexist during long periods of chronic infection without replacement. The characteristics of amino acid substitution in the HVR were not consistent with the random accumulation of mutations and imply that amino acid replacement in the HVR was strongly constrained. Another variable region of E2 centered on codon 60 shows similar constraints, while HVR2 was relatively unconstrained. Several of these features are difficult to explain if a neutralizing immune response against the HVR is the only selective force operating on E2. The impact of PCR artifacts such as nucleotide misincorporation and the shuffling of dissimilar templates is discussed.
Assuntos
Hepacivirus/genética , Hepatite C/virologia , Proteínas do Envelope Viral/genética , Sequência de Aminoácidos , Estudos de Coortes , Evolução Molecular , Feminino , Humanos , Dados de Sequência Molecular , Filogenia , Análise de SequênciaRESUMO
This look-back study was undertaken to identify newborn infants who had been infected with the hepatitis C virus (HCV) as a result of transfusions received before the introduction of routine screening in 1991 and to determine the transmission rates and persistence of transfusion-transmitted HCV infection acquired in the neonatal period. A total of 24 infants, transfused between 1980 and 1991, were identified as having received potentially infected blood from 11 blood donors. Ten of the donors had been administered batches of anti-D in 1977 known to have transmitted HCV genotype 1b infection. HCV RNA was detected in five of these donors when tested in 1994-95; the past donations of five of the donors, who had received anti-D immunoglobulin and had serological evidence of previous HCV infection but who were PCR negative when tested in 1994-95, were considered of lower risk. The source and time of acquisition of HCV infection for the one remaining donor in the study was not determined. Twenty-one (88%) of the 24 children were living at time of lookback. The median age at transfusion was 12 days. The median age at time of testing was 6.3 years. One child, who tested negative, was excluded from further analysis of HCV transmission, due to incomplete transfusion records. Overall, 12 of 20 (60%) children tested were positive for anti-HCV and seven (35%) were HCV RNA positive. Twelve (71%) of the 17 recipients of viraemic blood were ELISA positive and seven (41%) were PCR positive. Resolved HCV infection, as determined by ELISA pos, RIBA pos or indeterminate and PCR negativity, occurred in five of 12 (42%). In many instances there was more than one recipient per HCV infected donation. All of the reported children are clinically asymptomatic. However, the duration of HCV infection is relatively short and there is evidence of a degree of hepatitis in five of the seven children who are HCV RNA positive as judged by mildly elevated transaminase levels. The three who have undergone liver biopsy show mild hepatitis. The lower rates of persistence of HCV infection in this study may be due to the young age at exposure or to the source of infection which for all but one of the children was linked to one HCV genotype from female donors. Sharing of units of blood among multiple infants should be discouraged.
Assuntos
Hepatite C/epidemiologia , Hepatite C/transmissão , Reação Transfusional , Adolescente , Anticorpos Antivirais/sangue , Doadores de Sangue/estatística & dados numéricos , Criança , Pré-Escolar , Feminino , Hepacivirus/genética , Hepacivirus/imunologia , Hepacivirus/isolamento & purificação , Humanos , Lactente , Recém-Nascido , Irlanda/epidemiologia , Masculino , RNA Viral/sangue , Estudos Retrospectivos , Imunoglobulina rho(D)/efeitos adversos , Fatores de RiscoRESUMO
Hepatitis C virus (HCV) genotype 6a is found in a restricted part of South East Asia, including Hong Kong, Macau and Vietnam. We determined the full length coding sequence of a type 6a isolate (EUHK2) obtained from a Hong Kong blood donor. The sequence of EUHK2 contained a single open reading frame coding for a polyprotein of 3018 amino acids, within the range of 3008 to 3037 for other HCV genotypes. The full length sequence of EUHK2 showed 30.3%-32.9% nucleotide (24.3%-29.4% amino acid) sequence divergence from genotypes 1-4, but only 27.7% (20.7% amino acid) divergence from JK046 ("type 11a"). These similarity values were intermediate between those of other HCV genotypes (minimum 28.4%) and between subtypes (maximum 25%). The close evolutionary relationship of EUHK2 with JK046 was further indicated by their grouping together by phylogenetic analysis.
Assuntos
Hepacivirus/genética , Clonagem Molecular , DNA Viral/genética , Evolução Molecular , Genótipo , Hepacivirus/classificação , Hepacivirus/isolamento & purificação , Hong Kong , Humanos , Dados de Sequência Molecular , Fases de Leitura Aberta , Filogenia , Reação em Cadeia da Polimerase , Homologia de Sequência de Aminoácidos , Proteínas Virais/genéticaRESUMO
Detection of antibody to recombinant proteins derived from hepatitis C virus (HCV) genotype 1 represents the principal method for diagnosis of HCV infection. A method was developed for quantifying antibody reactivity in two third-generation enzyme immunoassays (Ortho EIA 3.0 and Murex VK48), and the influence of viraemia, HCV genotype, and host factors such as age, gender, and risk group upon antibody levels were investigated in a consecutive series of 117 anti-HCV-positive volunteer blood donors. Viraemic donors (as assessed by the polymerase chain reaction; PCR) showed significantly higher levels of anti-HCV by the Ortho EIA than those who were nonviraemic (adjusted mean difference of 10.1 fold after multiple regression analysis). The only other factor to influence significantly antibody level was genotype, where it was found that donors infected with type 1 showed 4 to 4.5 times greater serological reactivity by the Ortho assay than those infected with type 2 or 3. Antibody levels by the Ortho assay correlated closely to those detected by the Murex VK48 assay, and similar differences between PCR-positive and negative donors and between those infected with different genotypes were found. Differences in serological reactivity between genotypes indicate that a large proportion of epitopes of the type 1a or 1b recombinant proteins used in current assays are genotype specific. Variation in sensitivity of screening assays for different genotypes is of potential concern when used in countries where non-type 1 genotypes predominate in the blood donor or patient population.
Assuntos
Hepacivirus/imunologia , Anticorpos Anti-Hepatite C/imunologia , Técnicas Imunoenzimáticas , Alanina Transaminase/sangue , Doadores de Sangue , Genótipo , Hepacivirus/isolamento & purificação , Anticorpos Anti-Hepatite C/sangue , Humanos , Kit de Reagentes para Diagnóstico , ViremiaRESUMO
A disulfide bond that is evidently conserved in the guanine nucleotide-binding protein-coupled receptors is present in rhodopsin between Cys-110 and Cys-187. We have replaced these two cysteine residues by alanine residues and now report on the properties of the resulting rhodopsin mutants. The mutant protein C110A/C187A expressed in COS cells resembles wild-type rhodopsin in the ground state. It folds correctly to bind 11-cis-retinal and form the characteristic rhodopsin chromophore. It is inert to hydroxylamine in the dark, and its stability to dark thermal decay is reduced, relative to that of the wild type, by a delta delta G not equal to of only -2.9 kcal/mol. Further, the affinities of the mutant and wild-type rhodopsins to the antirhodopsin antibody rho4D2 are similar, both in the dark and in light. However, the metarhodopsin II (MII) and MIII photointermediates of the mutant are less stable than those formed by the wild-type rhodopsin. Although the initial rates of transducin activation are the same for both mutant and wild-type MII intermediates at 4 degrees C, at 15 degrees C the MII photointermediate in the mutant decays more than 20 times faster than in wild type. We conclude that the disulfide bond between Cys-110 and Cys-187 is a key component in determining the stability of the MII structure and its coupling to transducin activation.
Assuntos
Rodopsina/química , Rodopsina/fisiologia , Alanina/química , Sequência de Aminoácidos , Animais , Bovinos , Cisteína/química , Dissulfetos , Nucleotídeos de Guanina/metabolismo , Glicoproteínas de Membrana/química , Dados de Sequência Molecular , Mutagênese Sítio-Dirigida , Desnaturação Proteica , Proteínas Recombinantes , Rodopsina/imunologia , Opsinas de Bastonetes/química , Relação Estrutura-Atividade , Temperatura , Transducina/metabolismoRESUMO
Studies are reported on the inhibition of phospholipase A2 (PLA2) from porcine pancreas, cobra (Naja naja) venom, and the P388D1 macrophage-like cell line by human recombinant lipocortin I and bovine lung calpactin I. Membrane vesicles prepared from 1-stearoyl,2-arachidonoyl phosphatidylcholine (PC) and other PCs were utilized as substrate. Binding studies using sucrose flotation gradients showed that both lipocortin I and calpactin I bind to these vesicles although less tightly than to vesicles prepared from anionic phospholipids or fatty acids. Binding to PC was somewhat enhanced by Ca2+. Inhibition of cobra venom PLA2 was not observed when PC vesicles were used as substrate but was when dipalmitoyl phosphatidylethanolamine was used. Both the pancreatic and macrophage enzymes were inhibited when acting on PC. Interestingly, the inhibition of the macrophage enzyme toward PC depended on the fatty acid attached to the sn-2 position of PC with arachidonate greater than oleate greater than palmitate. Inhibition was also highest at low [PC]; these inhibition results can be explained by the "substrate depletion model" (Davidson, F. F., Dennis, E. A., Powell, M., and Glenney, J. (1987) J. Biol. Chem. 262, 1698-1705). Experimental and theoretical considerations suggest that the in vitro inhibition by lipocortins of this macrophage PLA2 from a cell that makes lipocortin and is active in prostaglandin production is due to effects on substrate availability rather than direct inhibition.
Assuntos
Proteínas de Ligação ao Cálcio/metabolismo , Venenos Elapídicos/análise , Lipossomos/metabolismo , Macrófagos/enzimologia , Pâncreas/enzimologia , Fosfolipases A/metabolismo , Fosfolipases/metabolismo , Animais , Anexinas , Ácido Araquidônico , Ácidos Araquidônicos/metabolismo , Cálcio/farmacologia , Proteínas de Ligação ao Cálcio/farmacologia , Linhagem Celular , Ácidos Graxos/metabolismo , Cinética , Ácido Oleico , Ácidos Oleicos/metabolismo , Ácido Palmítico , Ácidos Palmíticos/metabolismo , Fosfatidilcolinas/metabolismo , Fosfolipases A/antagonistas & inibidores , Fosfolipases A2 , SuínosRESUMO
Baseline cardiovascular risk factor variables were obtained from 1,041 black District of Columbia children in Grades 4-6 as part of a Know Your Body evaluation project. Screening included height, weight, triceps skinfold measurements, systolic and diastolic blood pressures, step-test for fitness, serum cholesterol, high-density lipoprotein cholesterol and thiocyanate. Results were compared with those in three other Know Your Body studies, Bronx, New York, Westchester, New York, and Los Angeles, and indicated that District of Columbia black children are more likely to have high cholesterol levels and to fail the fitness test than black children in the other studies. In the District of Columbia, obese children had significantly higher total serum cholesterol, systolic, diastolic, and high-density lipoprotein levels, and were less fit than other District of Columbia children; almost three-fourths of all of the children had one or more risk factors. Socioeconomic status was negatively correlated with diastolic blood pressure, skinfold thickness, and cholesterol levels and was positively correlated with high-density lipoprotein cholesterol. Rates of obesity and diastolic blood pressure were consistent with Bronx and Westchester comparisons suggesting that socioeconomic status interacts with ethnicity to determine risk factor levels. The existence of children with multiple risk factors in all of the Know Your Body studies supports the need for early intervention.
Assuntos
Negro ou Afro-Americano , Doenças Cardiovasculares/epidemiologia , Adolescente , Antropometria , California , Criança , Colesterol/sangue , Currículo , District of Columbia , Feminino , Promoção da Saúde , Humanos , Estudos Longitudinais , Masculino , Programas de Rastreamento , New York , Aptidão Física , Fatores de RiscoRESUMO
Non-denaturing polyacrylamide gel electrophoresis and non-denaturing agarose gel electrophoresis have been used to resolve [3H]R5020-binding components from chick oviduct cytosol. From both gel systems 2 peaks of bound radioactivity are resolved which display these properties of authentic progesterone receptor: binding of R5020: steroid specificity, saturability, and restriction to target tissues. The two peaks are approximately equal in magnitude, and there is no evidence for interconversion of the 2 peaks. The presence or absence of 10-20 mM sodium molybdate during cytosol preparation had no effect on the magnitude or mobility of either peak. Neither peak contains salt-dissociable components which affect its electrophoretic properties, suggesting a possible alteration of native receptor forms during electrophoresis.
Assuntos
Oviductos/metabolismo , Receptores de Progesterona/metabolismo , Animais , Galinhas , Citosol/metabolismo , Dietilestilbestrol/farmacologia , Eletroforese em Gel de Ágar/métodos , Eletroforese em Gel de Poliacrilamida/métodos , Feminino , Oviductos/efeitos dos fármacos , Promegestona/metabolismo , Desnaturação Proteica , Receptores de Progesterona/efeitos dos fármacos , Receptores de Progesterona/isolamento & purificaçãoRESUMO
The origin of and relationships among multiple forms of the estrogen receptor from rat uteri were investigated using electrophoretic and conventional hydrodynamic methods of analysis. Evidence is presented that the molybdate-stabilized, multimeric receptor (Stokes radius approximately 70A; S20,w approximately 9.5 S; Mr approximately 290,000) corresponds to an acidic form of the receptor that has relatively high electrophoretic mobility. This discrete form, which appears to represent the untransformed state that does not bind to DNA, was converted to a number of derived forms by exposure to conditions that result in receptor transformation and/or subunit dissociation. In crude cytosol, transformation always generated receptor forms that were excluded from polyacrylamide gels, and it was shown that these are large heterogeneous aggregates. This explains previous failed attempts to analyze the receptor by polyacrylamide gel electrophoresis. Transformation of partially purified, molybdate-stabilized receptor never led to aggregate formation, but resulted instead in the generation of two relatively basic estrogen-binding species of low electrophoretic mobility. These components may represent the free or dissociated estrogen-binding subunits. Together, the results suggest a model for the molybdate-stabilized receptor wherein at least one of its components is an acidic, nonestrogen-binding subunit.
Assuntos
Receptores de Estrogênio/isolamento & purificação , Útero/metabolismo , Animais , Estabilidade de Medicamentos , Estradiol/metabolismo , Feminino , Substâncias Macromoleculares , Peso Molecular , Molibdênio/farmacologia , Ratos , Receptores de Estrogênio/efeitos dos fármacos , Receptores de Estrogênio/metabolismoRESUMO
Conditions are defined which permit analysis of estrogen receptors from the mammalian uterus by polyacrylamide gel electrophoresis, thereby solving a longstanding problem encountered in previous attempts at such analysis, namely the failure of a large portion of the receptor population to enter such gels. A paramount requirement for entry of the estrogen-receptor complex into polyacrylamide gels is its maintenance in an untransformed state which does not form aggregates that are excluded from these gels. Of the multiple estrogen-binding proteins separated, only one (relative mobility of 0.5-0.6) possessed the definitive characteristics of the classical estrogen receptor. The inclusion of molybdate in extraction buffers selectively enhanced receptor recovery and facilitated its separation. Moreover, the estrogen-receptor complex so resolved is separated from other types of estrogen-binding proteins present in the uterine cytosol. These findings show that the molybdate-stabilized estrogen receptor exists in a single discrete form, but otherwise exhibits multiple forms that are probably artifactual. Electrophoresis in discontinuous buffers, but not in a continuous buffer system, promoted aggregate formation. This finding has implications concerning the subunit structure of the untransformed receptor.
Assuntos
Molibdênio/farmacologia , Receptores de Estrogênio/análise , Animais , Eletroforese em Gel de Poliacrilamida , Estradiol/metabolismo , Feminino , Cinética , Ratos , Ratos Endogâmicos , Distribuição Tecidual , Útero/análiseRESUMO
From the inserts of two recombinant plasmids isolated from a murine liver cDNA library, the nucleotide sequence coding for the C3 alpha chain was obtained and the corresponding amino acid sequence was derived. The alpha chain portion of the mRNA is 2979 nucleotides long, specifying a polypeptide of 993 amino acids. The molecular weight of the alpha chain, in the absence of carbohydrate, was calculated from the sequence data to be 112,933. Two possible carbohydrate attachment sites were predicted at residues 269 (Asn) and 947 (Asn). In addition, the positions for two putative factor I cleavage sites were predicted from a comparison with the cleavage sites in the human C3 alpha chain. The C3 alpha chain contains 24 cysteine residues, 10 of these clustered in the C-terminal 175 amino acids of the alpha chain. Together with the accompanying report (Lundwall, A, Wetsel, R.A., Domdey, H., Tack, B.F., and Fey, G.H. (1984) J. Biol. Chem. 259, 13851-13856), this study completes the nucleotide and amino acid structure of the murine precursor prepro-C3 molecule.
Assuntos
Complemento C3/genética , DNA/análise , Sequência de Aminoácidos , Animais , Sequência de Bases , Clonagem Molecular , Códon/análise , Enzimas de Restrição do DNA/metabolismo , Fígado/análise , Camundongos , Peso MolecularRESUMO
An epidemiological survey was carried out among high school students of 3 French regions. Their use of drugs (alcohol, tobacco, psychotropic drugs, illicit drugs) was studied, as well as their self-perception of personality, relations inside and outside the family, school performance, and lifestyle. Different aspects of drinking were considered: regularity of intake, quantity absorbed, inebriation. The use of alcoholic drinks together with psychotropic substances was studied. A cluster analysis applied to adolescent personality self-perception revealed 10 different personality types (5 for the boys; 5 for the girls). The social, family, and relational characteristics of each personality type are described. The correlations between personality self-perception and liquor use allow us to define 3 profiles of heavy drinkers.
Assuntos
Consumo de Bebidas Alcoólicas , Personalidade , Psicologia do Adolescente , Transtornos Relacionados ao Uso de Substâncias/epidemiologia , Logro , Adolescente , Adulto , Família , Feminino , Humanos , Relações Interpessoais , Estilo de Vida , Masculino , AutoimagemRESUMO
Further chemical evidence has been obtained using NaB3H4 to support our previous assignment of a thiol ester bond in human C3 (Tack, B. F., Harrison, R. A., Janatova, J., Thomas, M. L., and Prahl, J. W. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 5764-5768). Following trypsin activation of human C3 in the presence of NaB3H4, 3H was shown to have incorporated specifically into the alpha'-chain of C3b. Subsequent fragmentation of [3H]C3b with porcine elastase further localized the label to the C3d subdomain. Under identical conditions, native C3 or C3 pretreated with trypsin (C3b) showed low reactivity with NaB3H4. A tryptic peptide containing the 3H label was isolated following digestion of [3H]C3b on activated thiol-Sepharose. After hydrolysis and saponification of the peptide hydrolysate, amino acid analysis indicated that the 3H had been incorporated into alpha-amino-delta-hydroxyvaleric acid, the product expected from reduction of an ester bond involving a glutamyl residue. On sequence analysis of the labeled peptide, the 3H was shown to reside at the position of the glutamyl residue previously proposed to be involved in the thiol ester bond. The residue at this position was confirmed as alpha-amino-delta-[3H] hydroxyvaleric acid by high performance liquid chromatography analysis and, after back hydrolysis, by amino acid analysis. These data significantly strengthen earlier studies which indicated the presence of a beta-Cys-gamma-Glu thiol ester bond in human C3.