J L Oliver, J M Martinez-Zapater, L Pascual, A M Enriquez, C Ruiz-Rejón, M Ruiz-Rejón
{"title":"Different genome amplification mechanisms and duplicate gene expression in Liliaceae.","authors":"J L Oliver, J M Martinez-Zapater, L Pascual, A M Enriquez, C Ruiz-Rejón, M Ruiz-Rejón","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"10 ","pages":"341-63"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17414962","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The utilization of polymorphic enzymes in forensic science.","authors":"G F Sensabaugh","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"11 ","pages":"137-54"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17698204","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Chemical modification with pyridoxal 5'-phosphate as a tool in the study of ligand interactions in various lactate dehydrogenase isozymes.","authors":"P C Engel","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"7 ","pages":"151-9"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17935743","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Genetic and hormonal regulation of esterase 6 activity in male Drosophila melanogaster.","authors":"R C Richmond, C S Tepper","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The esterase 6 locus in Drosophila melanogaster is the structural gene for a carboxylesterase (E.C. 3.1.1.1) and is polymorphic for two major electrophoretic variants (slow and fast). Isogenic lines containing X chromosomes extracted from natural populations and substituted into a common genetic background were used to detect unlinked factors that affect the activity of the Est 6 locus. Twofold activity differences of esterase 6 were found among males from these derived lines, which differ only in their X chromosome. These unlinked activity modifiers identify possible regulatory elements. Immunoelectrophoresis was used to estimate quantitatively the levels of specific cross-reacting material in the derived lines. The results show that the variation in activity is due to differences in the amount of EST 6 present. Physiological studies of the control of EST 6 levels reveal that both juvenile hormone and 20 hydroxyecdysone stimulate the production of EST 6 activity in adult males. These results suggest that the effects of X chromosomes on EST 6 activity may be effected by modulating the level of adult hormone titers in Drosophila.</p>","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"9 ","pages":"91-106"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17473538","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Epigenetic formation of isozymes: The effect of aging.","authors":"R W Gracy","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"7 ","pages":"187-201"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17935744","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Isozymes of human phosphofructokinase: biochemical and genetic aspects.","authors":"S Vora","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human PFK is under the control of three structural loci that encode muscle-type (M), liver-type (L), and platelet-type (P) subunits. These loci are differentially expressed in various human tissues, resulting in a tissue-specific isozyme distribution patterns. Random tetramerization of these subunits produces various homotetrameric and heterotetrameric isozymes distinguishable by ion-exchange chromatography and subunit-specific mouse monoclonal antibodies. Inherited PFK deficiency is associated with five clinically and biochemically identifiable groups. The largest and best defined of these consists of the patients with glycogenosis type VII (group I). This syndrome results from a total deficiency of the catalytically active M subunit; the molecular pathology of the other four syndromes remains to be elucidated. Subunit- and species-specific hybridoma antibodies to the PFK subunits have permitted not only precise immunochemical analysis of this complex isozyme system, but also chromosomal localization of the PFK loci. In addition, immunochemical homologies among vertebrate PFKs determined using monoclonal antibodies suggest both an ancient duplication of the ancestral PFK gene and the structural conservatism of vertebrate PFK subunits despite this early divergence. Using somatic cell hybrids and subunit-specific antibodies, the PFKM, PFKP, and PFKL loci have been assigned to chromosomes I (region cen leads to q32), 10p and 21, respectively. The localization of PFKL to chromosome 21 and the chromatographic demonstration of a specific increase in the L subunit in red cells from trisomy 21 individuals has thus resolved the controversy about whether the previously observed elevation in PFK activity in Down syndrome represented a gene dosage effect. PFK exhibits both quantitative increases and isozymic shifts secondary to the altered gene expression in neoplasia. Since these alterations are correlated with the rate of growth and not the cell type of origin, PFK appears to be not only a transformation-linked but also a progression-linked discriminant of malignancy.</p>","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"11 ","pages":"3-23"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17290511","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Evolutionary affinities of plant phosphoglucose isomerase and fructose-1,6-bisphosphatase isozymes.","authors":"N F Weeden","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"8 ","pages":"53-66"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17375210","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
D A Wright, C M Richards, J S Frost, A M Camozzi, B J Kunz
{"title":"Genetic mapping in amphibians.","authors":"D A Wright, C M Richards, J S Frost, A M Camozzi, B J Kunz","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"10 ","pages":"287-311"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17414959","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The role of alcohol dehydrogenase and aldehyde dehydrogenase isozymes in alcohol metabolism, alcohol sensitivity, and alcoholism.","authors":"H W Goedde, D P Agarwal, S Harada","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Isozymes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were studied in human organs and tissues using sensitive analytical techniques. Both ADH and ALDH showed an extensive polymorphism among different racial groups. In liver extracts and other tissues of Japanese an isozyme of ALDH (ALDH I) with a low Km for acetaldehyde was found to be deficient. The ALDH isozyme deficiency might account for the marked initial sensitivity to alcohol in Orientals owing to their impaired acetaldehyde oxidizing capacity. Significantly low erythrocyte ALDH activity was noted more frequently in chronic alcoholics than in healthy controls. After subcellular fractionation of livers from alcoholics a preferential damage of mitochondrial ALDH isozyme was observed. The metabolism of acetaldehyde has received considerable attention in the past few years, owing to the toxic effects of this substance. Rapid progress has been made in the understanding of the multiple molecular forms of ADH and ALDH in human tissues. Our recent studies have demonstrated that the isozymes of ALDH may play an important role in the pathogenesis of alcohol-related organ damage and in the biological sensitivity to alcohol in certain ethnic groups. A possible protection of ALDH I deficiency against alcoholism in Japanese has been discussed. More recent reports [Imprain et al, 1982; Jones, 1982] indicate that, in addition to the enzymatically active ALDH II, tissues from Orientals deficient in ALDH I isozyme contain enzymatically inactive, immunologically cross-reactive material homologous with ALDH I. Thus, the absence of ALDH I isozyme is not due to a regulatory mutation, a gene deletion, or a nonsense mutation, but probably results from a structural mutation.(ABSTRACT TRUNCATED AT 250 WORDS)</p>","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"8 ","pages":"175-93"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17415769","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}