Isozymes最新文献

{"title":"Regulation of lactate dehydrogenase gene expression.","authors":"R A Jungmann, D F Derda, D C Kelley, M F Miles, D Milkowski, J S Schweppe","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"7 ","pages":"161-74"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17371674","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":"Cellular localization, metabolism, and physiology.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"8 ","pages":"1-269"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17684359","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":"Beta-hexosaminidase isozymes and replacement therapy in Gm2 gangliosidosis.","authors":"M C Rattazzi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The problem of cell targeting of lysosomal enzymes is a critical one in the development of strategies for therapeutic enzyme replacement in lysosomal storage diseases. In principle, posttranscriptional isozymes with different carbohydrate-chain composition may be helpful in exploiting existing glycosyl-specific receptors on target cells, if the receptor specificities are known and match the glycosyl composition of available isozymes. In practice, however, the choice is limited to isozymes that can be obtained from tissues available in abundance, such as placenta or blood plasma. Our early experiments show that one can interfere with the interaction between hepatic (RES) receptor and enzyme glycosyl chain, to obtain extrahepatic targeting of beta-hexosaminidase, with catabolic effects. This approach, of course, does not have an immediate therapeutic application, as it involves injection of large amounts of foreign material in order to inhibit hepatic uptake. Modification of the glycosyl chain may be the method of choice in selected instances [Furbish et al. 1981], but is applicability again depends on the knowledge of receptor specificity on target cells and on composition of the glycosyl chain of the enzyme in question. Our recent experiments are a first step toward obtaining enzyme forms that can be endocytosed efficiently by mechanisms that are independent of glycosyl-specific receptors. Charge-mediated, absorptive endocytosis can be obtained by covalent coupling of cationic PLL to beta-hexosaminidase. Given the abundance of negative surface charges on most cell types [Weiss, 1969], this approach may be applicable to different target cells and organs, and possibly also to lysosomal enzymes other than beta-hexosaminidase. The existence of glycosyl recognition signals on beta-hexosaminidase can be obviated by simple chemical manipulations, such as Na-metaperiodate oxidation, which effectively prevents hepatic RES uptake [Rattazzi et al, 1982]. In combination with PLL conjugation, this may ultimately result in an enzyme form that escapes the undesired, preferential RES uptake and is efficiently endocytosed by most cells. It will remain to be seen if this artificially created isozyme (for which we propose the name \"ersatzyme\") is catabolically effective. This can easily be verified in our animal model, along the lines followed to demonstrate the catabolic effects of native Hex A. Finally, the recent developments in molecular genetics, which allows production of human proteins in bacterial systems by recombinant DNA techniques, make it very likely that abundant beta-hexosaminidase may be similarly obtained for therapeutic applications.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"11 ","pages":"65-81"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17290512","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":"Molecular structure and regulation.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"7 ","pages":"1-324"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17698215","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":"Application of isozymes to the mapping of inherited ophthalmic disorders.","authors":"R E Ferrell,&nbsp;P P Majumder","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"11 ","pages":"121-35"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17377239","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":"Biochemical and clinical studies of aldolase isozymes in human cancer.","authors":"M Asaka,&nbsp;K Nagase,&nbsp;E Alpert","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Radioimmunoassays specific for ALD isozymes were developed for the quantification of human ALD-A, -B, and -C. The method is a double antibody radioimmunoassay consisting of purified radioiodinated ALD-A, -B, and C as ligand, chicken antibodies to ALD-A, -B, and -C, and rabbit antibodies to chicken IgG. The Iodogen method was used for the iodination of the purified isozymes. ALD-A was present in high concentration in muscle, ALD-B in adult liver, and ALD-C in adult brain. ALD-A was elevated in hepatoma tissue and hepatoma cell lines, whereas ALD-B was distinctly low. Normal serum levels for the three isozymes were determined. The ALD-A level in the serum from 41 normal subjects was 170 +/- 39 ng/ml. Serum ALD-A level was increased in many patients with cancer and muscle diseases, but not in patients with hepatitis or other benign diseases. Serum ALD-B level in 11 normal subjects was 28.5 +/- 9.2 ng/ml. Serum ALD-C level in 12 normal subjects was 2.4 +/- 0.7 ng/ml. The determination of ALD-A, -B, and -C by radioimmunoassay may be a valuable tool in biochemical and clinical studies of these isozymes.</p>","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"11 ","pages":"183-95"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17377240","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":"Induced somatic cell mutations detected in cultured cells by electrophoresis.","authors":"M J Siciliano,&nbsp;G M Adair,&nbsp;E N Atkinson,&nbsp;R M Humphrey","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"10 ","pages":"41-9"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17415765","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":"Molecular varieties of isozymes and their role in studies of gene regulation and expression during eukaryote development.","authors":"J G Scandalios","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"9 ","pages":"1-31"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17413404","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":"Analysis of creatine kinase isozymes during muscle differentiation.","authors":"H M Eppenberger,&nbsp;J C Perriard,&nbsp;T Wallimann","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"7 ","pages":"19-38"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17935745","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 multi-locus catalase gene-enzyme system of maize: a model system for the study of gene regulation and enzyme differentiation and function in higher plants.","authors":"A S Tsaftaris,&nbsp;J G Scandalios","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77729,"journal":{"name":"Isozymes","volume":"7 ","pages":"59-77"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17935748","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}