Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90291-3
K. Van Dam
{"title":"A possible explanation for the ATP “jump” observed on addition of ADP to mitochondria in State 4","authors":"K. Van Dam","doi":"10.1016/0926-6569(64)90291-3","DOIUrl":"10.1016/0926-6569(64)90291-3","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 181-183"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90291-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795497","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90294-9
Anthony T. Tu
{"title":"Hemediglutathione, a synthetic compound with peroxidase-like activity","authors":"Anthony T. Tu","doi":"10.1016/0926-6569(64)90294-9","DOIUrl":"10.1016/0926-6569(64)90294-9","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 191-193"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90294-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795501","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90285-8
Ronald A. Butow, Walter L. Nelson
{"title":"Respiratory control in guinea-pig-mammary gland mitochondria","authors":"Ronald A. Butow, Walter L. Nelson","doi":"10.1016/0926-6569(64)90285-8","DOIUrl":"10.1016/0926-6569(64)90285-8","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 166-168"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90285-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795491","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90286-X
N.H. Sloane , D.W. Mercer, M. Danoff
{"title":"Phosphoglucomutase: a model for active-site characterization I. Amino acid composition","authors":"N.H. Sloane , D.W. Mercer, M. Danoff","doi":"10.1016/0926-6569(64)90286-X","DOIUrl":"10.1016/0926-6569(64)90286-X","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 168-170"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90286-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795492","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90278-0
R.H. Bauerle, M. Freundlich, F.C. Størmer, H.E. Umbarger
Acetohydroxy acid synthetase, which catalyzes the synthesis of α-acetolactate and α-acetohydroxybutyrate, the first 5- and 6-carbon precursors of valine and isoleucine, respectively, has been studied in extracts of Salmonella typhimurium. Required for enzyme activity are thiamine pyrophosphate, Mg2+ and an unidentified factor which can be supplied by boiled extracts of Salmonella or yeast. The activity of the enzyme is inhibited by l-valine and a group of related compounds. Valine inhibition is noncompetitive with respect to pyruvate and thiamine pyrophosphate and is rigidly dependent on pH. Inhibition is greatest at pH 8.0, also the optimal pH for activity, and is non-existent at values less than 6.5. The sensitivity of the enzyme to valine can be removed by heat, Hg2+ or urea treatments. Glutathione is effective in restoring valine sensitivity to the Hg2+-treated enzyme. These properties indicate that this enzyme belongs to the class of proteins recently described as “allosteric” in nature.
{"title":"Control of isoleucine, valine and leucine biosynthesis","authors":"R.H. Bauerle, M. Freundlich, F.C. Størmer, H.E. Umbarger","doi":"10.1016/0926-6569(64)90278-0","DOIUrl":"10.1016/0926-6569(64)90278-0","url":null,"abstract":"<div><p>Acetohydroxy acid synthetase, which catalyzes the synthesis of α-acetolactate and α-acetohydroxybutyrate, the first 5- and 6-carbon precursors of valine and isoleucine, respectively, has been studied in extracts of <em>Salmonella typhimurium</em>. Required for enzyme activity are thiamine pyrophosphate, Mg<sup>2+</sup> and an unidentified factor which can be supplied by boiled extracts of Salmonella or yeast. The activity of the enzyme is inhibited by <sup>l</sup>-valine and a group of related compounds. Valine inhibition is noncompetitive with respect to pyruvate and thiamine pyrophosphate and is rigidly dependent on pH. Inhibition is greatest at pH 8.0, also the optimal pH for activity, and is non-existent at values less than 6.5. The sensitivity of the enzyme to valine can be removed by heat, Hg<sup>2+</sup> or urea treatments. Glutathione is effective in restoring valine sensitivity to the Hg<sup>2+</sup>-treated enzyme. These properties indicate that this enzyme belongs to the class of proteins recently described as “allosteric” in nature.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 142-149"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90278-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84431980","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90268-8
Hyman Hartman , Alvin I. Krasna
1.
1. The adaptation of hydrogenase (EC 1.98.1.1) in Scenedesnus obliquus was inhibited by dithionite, sulfite, arsenite, marphaside, BAL, 2,2′-dipyridyl, and 1,10-phenanthroline. None of these inhibitors had any effect on the active hydrogenase after adaptation.
2.
2. The active hydrogenase of Scenedesmus was inhibited by silver, mercury, and cupric ions, p-chloromercuribenzoate and iodoacetamide. The silver and mercury inhibition could be reversed by BAL.
3.
3. The hydrogenase of Proteus vulgaris was not affected by the inhibitors of the adaptation process but was inhibited by those reagents which inhibited the active hydrogenase of Scenedesmus.
{"title":"Properties of the hydrogenase of scenedesmus","authors":"Hyman Hartman , Alvin I. Krasna","doi":"10.1016/0926-6569(64)90268-8","DOIUrl":"10.1016/0926-6569(64)90268-8","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The adaptation of hydrogenase (EC 1.98.1.1) in <em>Scenedesnus obliquus</em> was inhibited by dithionite, sulfite, arsenite, marphaside, BAL, 2,2′-dipyridyl, and 1,10-phenanthroline. None of these inhibitors had any effect on the active hydrogenase after adaptation.</p></span></li><li><span>2.</span><span><p>2. The active hydrogenase of Scenedesmus was inhibited by silver, mercury, and cupric ions, <em>p</em>-chloromercuribenzoate and iodoacetamide. The silver and mercury inhibition could be reversed by BAL.</p></span></li><li><span>3.</span><span><p>3. The hydrogenase of <em>Proteus vulgaris</em> was not affected by the inhibitors of the adaptation process but was inhibited by those reagents which inhibited the active hydrogenase of Scenedesmus.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 52-58"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90268-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23793356","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90274-3
Monique Monnot, Jeannine Yon
The tryptic hydrolysis of lactoglobulins A and B is followed for different pH values. The variations of the kinetic contants according to the pH, give us some information on the reaction mechanism. During the intermediary complex formation, the enzyme associating with the lactoglobulin (A or B form) induces the Tanford transformation of the substrate molecule with demasking of the anomalous carboxylic groups thereby facilitating their ionization.
{"title":"Étude cinétique comparée de l'hydrolyse trypsique des lactoglobulines A et B fonction du pH","authors":"Monique Monnot, Jeannine Yon","doi":"10.1016/0926-6569(64)90274-3","DOIUrl":"10.1016/0926-6569(64)90274-3","url":null,"abstract":"<div><p>The tryptic hydrolysis of lactoglobulins A and B is followed for different pH values. The variations of the kinetic contants according to the pH, give us some information on the reaction mechanism. During the intermediary complex formation, the enzyme associating with the lactoglobulin (A or B form) induces the <span>Tanford</span> transformation of the substrate molecule with demasking of the anomalous carboxylic groups thereby facilitating their ionization.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 105-110"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90274-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88920508","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90289-5
A.O.M. Stoppani, A. Bennun, E.M. De Pahn
{"title":"Energy requirement for the anaerobic oxidation of acetate in baker's yeast","authors":"A.O.M. Stoppani, A. Bennun, E.M. De Pahn","doi":"10.1016/0926-6569(64)90289-5","DOIUrl":"10.1016/0926-6569(64)90289-5","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 176-178"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90289-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74618489","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90296-2
Elizabeth R. Simons, Elkan R. Blout
{"title":"The effect of proteolytic enzymes on synthetic polypeptides","authors":"Elizabeth R. Simons, Elkan R. Blout","doi":"10.1016/0926-6569(64)90296-2","DOIUrl":"10.1016/0926-6569(64)90296-2","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 197-199"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90296-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795503","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}