Isozymes最新文献

{"title":"The antioxidant enzyme genes Cat and Sod of maize: regulation, functional significance, and molecular biology.","authors":"J G Scandalios","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"14 ","pages":"19-44"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14425652","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 use of isozyme loci as markers in transferring genes for disease resistance in plants.","authors":"D E McMillin, R E Allan","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"16 ","pages":"145-55"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14429099","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 and the regulatory structure of the genome.","authors":"C L Markert","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"14 ","pages":"1-17"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14425648","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":"Peanut peroxidase: a model system for peroxidase analysis.","authors":"R B van Huystee, R N Chibbar","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"13 ","pages":"155-79"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14705321","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":"Agriculture, physiology, and medicine. Proceedings of the 5th International Congress on Isozymes. 3. Kos, Greece, May 26-29, 1986.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"16 ","pages":"1-281"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14732329","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":"Genes and proteins of chicken creatine kinase isozymes: developmental regulation and functional significance.","authors":"J C Perriard, H M Eppenberger, J P Hossle, B Schäfer","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"14 ","pages":"83-101"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14425654","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":"Structure and function of adenylate kinase isozymes in normal humans and muscular dystrophy patients.","authors":"M Hamada,&nbsp;H Takenaka,&nbsp;K Fukumoto,&nbsp;S Fukamachi,&nbsp;T Yamaguchi,&nbsp;M Sumida,&nbsp;T Shiosaka,&nbsp;Y Kurokawa,&nbsp;H Okuda,&nbsp;S A Kuby","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Two isozymes of adenylate kinase from human Duchenne muscular dystrophy serum, one of which was an aberrant form specific to DMD patients, were separated by Blue Sepharose CL-6B affinity chromatography. The separated aberrant form possessed a molecular weight of 98,000 +/- 1,500, whereas the normal serum isozyme had a weight of 87,000 +/- 1,600, as determined by SDS-polyacrylamide gel electrophoresis, gel filtration, and sedimentation equilibrium. The sedimentation coefficients were 5.8 S and 5.6 S for the aberrant form and the normal form, respectively. Both serum isozymes are tetramers. The subunit size of the aberrant isozyme (Mr = 24,700) was very similar to that of the normal human liver isozyme, and the subunit size of the normal isozyme (Mr = 21,700) was very similar to that of the normal human muscle enzyme. The amino acid composition of the normal serum isozyme was similar to that of the muscle-type enzyme, and that of the aberrant isozyme was similar to that of the liver enzyme, with some exceptions in both cases.</p>","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"16 ","pages":"81-99"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14171298","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":"Lipoxygenase isozymes in higher plants: biochemical properties and physiological role.","authors":"A J Mack, T K Peterman, J N Siedow","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"13 ","pages":"127-54"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14239459","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":"Structure and expression of human and rat aldolase isozyme genes: multiple mRNA species of aldolase A produced from a single gene.","authors":"K Hori,&nbsp;T Mukai,&nbsp;K Joh,&nbsp;Y Arai,&nbsp;M Sakakibara,&nbsp;H Yatsuki","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"14 ","pages":"153-75"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14425650","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":"X-linked gene expression and X-chromosome inactivation: marsupials, mouse, and man compared.","authors":"J L VandeBerg,&nbsp;E S Robinson,&nbsp;P B Samollow,&nbsp;P G Johnston","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The existence of paternal X inactivation in Australian and American marsupial species suggests that this feature of X-chromosome dosage compensation is not a recent adaptation, but probably predates the evolutionary separation of the Australian and American marsupial lineages. Although it is theoretically possible that the marsupial system is one of random X inactivation with p greater than 0.99 and q less than 0.01 and dependent on parental source, no instance of random X inactivation (p = q or p not equal to q) has ever been verified in any tissue or cell type of any marsupial species. Therefore, we conclude that the most fundamental difference in X inactivation of marsupials and eutherians is whether the inactive X is the paternal one or is determined at random (with p = q in most but not all cases). The only other unequivocal difference between eutherians and marsupials is that both X chromosomes are active in mice and human oocytes, but not in kangaroo oocytes. Apparently, the inactive X is reactivated at a later meiotic stage or during early embryogenesis in kangaroos. X-chromosome inactivation takes place early in embryogenesis of eutherians and marsupials. Extraembryonic membranes of mice exhibit paternal X inactivation, whereas those of humans seem to exhibit random X inactivation with p greater than q (i.e., preferential paternal X inactivation). In general, extraembryonic membranes of marsupial exhibit paternal X inactivation, but the Gpd locus is active on both X chromosomes in at least some cells of kangaroo yolk sac. It is difficult to draw any general conclusion because of major differences in embryogeny of mice, humans, and marsupials, and uncertainties in interpreting the data from humans. Other differences between marsupials and eutherians in patterns of X-linked gene expression and X-chromosome inactivation seem to be quantitative rather than qualitative. Partial expression of some genes on the inactive X is characteristic of marsupials, with species variation in the behavior of specific loci; some X-linked human genes on the inactive chromosome also are known to exhibit partial activity in vivo and in cultured cells. The X chromosomes of marsupials do not behave as units with respect to transcriptional activity, nor does the human X chromosome. In addition, Barr bodies have recently been detected at interphase in some marsupials, establishing that this manifestation of X chromosome inactivity is not restricted to eutherians.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"15 ","pages":"225-53"},"PeriodicalIF":0.0,"publicationDate":"1987-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14425661","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}