{"title":"Coupled oscillator theory of enzyme action.","authors":"M D Williams, J L Fox","doi":"10.1007/978-3-642-81503-4_7","DOIUrl":"https://doi.org/10.1007/978-3-642-81503-4_7","url":null,"abstract":"","PeriodicalId":19093,"journal":{"name":"Molecular biology, biochemistry, and biophysics","volume":"32 ","pages":"86-96"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-3-642-81503-4_7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18453892","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":"Three multifunctional protein kinase systems in transmembrane control.","authors":"Y Nishizuka","doi":"10.1007/978-3-642-81503-4_9","DOIUrl":"https://doi.org/10.1007/978-3-642-81503-4_9","url":null,"abstract":"","PeriodicalId":19093,"journal":{"name":"Molecular biology, biochemistry, and biophysics","volume":"32 ","pages":"113-35"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17317979","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}
S Ebashi, Y Nonomura, K Kohama, T Kitazawa, T Mikawa
{"title":"Regulation of muscle contraction by Ca ion.","authors":"S Ebashi, Y Nonomura, K Kohama, T Kitazawa, T Mikawa","doi":"10.1007/978-3-642-81503-4_14","DOIUrl":"https://doi.org/10.1007/978-3-642-81503-4_14","url":null,"abstract":"","PeriodicalId":19093,"journal":{"name":"Molecular biology, biochemistry, and biophysics","volume":"32 ","pages":"183-94"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17175510","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":"Structural and dynamic aspects of recognition between tRNAs and aminoacyl-tRNA synthetases.","authors":"D G Knorre, V V Vlassov","doi":"10.1007/978-3-642-81503-4_22","DOIUrl":"https://doi.org/10.1007/978-3-642-81503-4_22","url":null,"abstract":"","PeriodicalId":19093,"journal":{"name":"Molecular biology, biochemistry, and biophysics","volume":"32 ","pages":"278-300"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18052027","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":"Suicide substrates: mechanism-based inactivators of specific target enzymes.","authors":"C Walsh","doi":"10.1007/978-3-642-81503-4_5","DOIUrl":"https://doi.org/10.1007/978-3-642-81503-4_5","url":null,"abstract":"","PeriodicalId":19093,"journal":{"name":"Molecular biology, biochemistry, and biophysics","volume":"32 ","pages":"62-77"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18453891","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}
E R Stadtman, R J Hohman, J N Davis, M Wittenberger, P B Chock, S G Rhee
{"title":"Subunit interaction of adenylylated glutamine synthetase.","authors":"E R Stadtman, R J Hohman, J N Davis, M Wittenberger, P B Chock, S G Rhee","doi":"10.1007/978-3-642-81503-4_11","DOIUrl":"https://doi.org/10.1007/978-3-642-81503-4_11","url":null,"abstract":"<p><p>The glutamine synthetase (GS) activity in Escherichia coli is regulated by a bicyclic interconvertible enzyme cascade which involves the cyclic adenylylation (inactivation) and deadenylylation (activation) of GS on the one hand, and the modulation of these processes by the uridylylation and deuridylylation of Shapiro's regulatory protein on the other. The specific activity of GS in a given metabolic state is determined by the fraction of its subunits that are adenylylated, and this fraction is determined by the concentration of over 40 metabolites. Through allosteric and substrate interactions with one or more of the cascade enzymes, these metabolites alter the rates of the covalent modification and demodification reactions. By means of immunoprecipitation studies with anti-AMP specific antibodies, it has been established that the partially adenylylated glutamine synthetase, which is present in a given steady state, is a mixture of hybrid molecules containing different numbers and possibly distributions of adenylylated subunits. Partial separation of these hybrid mixtures has been achieved by affinity chromatography on Affi-Blue Sepharose columns. From immunochemical studies it is evident that anti-AMP antibodies can react with adenylylated subunits of all molecular species of GS, but that the capacities of these primary antigen-antibody reactions to yield precipitable aggregates is very dependent of the number of adenylylated subunits per molecule, and much less so upon the total concentration of adenylylated subunits present. the studies suggest that precipitability is a function either of the distribution of adenylylated subunits within hybrid species, or of the kinetics of intra- vs intermolecular bivalent interactions.</p>","PeriodicalId":19093,"journal":{"name":"Molecular biology, biochemistry, and biophysics","volume":"32 ","pages":"144-56"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17175508","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":"Effect of catabolite repression on chemotaxis in Salmonella typhimurium.","authors":"D E Koshland, M J Anderson","doi":"10.1007/978-3-642-81503-4_10","DOIUrl":"https://doi.org/10.1007/978-3-642-81503-4_10","url":null,"abstract":"<p><p>The chemotaxis of Salmonella typhimurium LT2-ST1, grown with different sole carbon sources toward ribose, allose, serine, aspartate, and glucose, was examined. Maximum chemotaxis toward serine, aspartate, and glucose were unchanged with either glucose or citrate as the carbon source. The height of the peak in the ribose response curve was 25% of a standard serine response when the bacteria were grown on citrate. However, when the bacteria were grown on glucose, the ribose response was 1% of the serine standard, and when on glycerol, 5%. Chemotaxis toward allose, a competitive inhibitor of ribose chemotaxis, was similarly affected. The amount of ribose binding protein, the receptor for ribose chemotaxis, was determined in bacteria grown on citrate, glucose, or glycerol. The amount of ribose-binding protein released from cells grown on glucose or glycerol was appreciably less than the amount released from cells grown on citrate. These data suggest that the observed effect on ribose chemotaxis is due to catabolite repression of ribose-binding protein and another component of the chemotactic system.</p>","PeriodicalId":19093,"journal":{"name":"Molecular biology, biochemistry, and biophysics","volume":"32 ","pages":"136-43"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17830823","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}