{"title":"Prothrombin activation with cathepsin C","authors":"Geraldine M. Purcell, Marion I. Barnhart","doi":"10.1016/0006-3002(63)91067-9","DOIUrl":"10.1016/0006-3002(63)91067-9","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 800-802"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91067-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673164","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":"Réaction phosphoroclastique du pyruvate par Clostridium saccharobutyricum Mise en évidence de l'intervention d'un cofacteur de nature ptéridique dans la dégradation du pyruvate","authors":"Colette Delavier-Klutchko","doi":"10.1016/0006-3002(63)91022-9","DOIUrl":"10.1016/0006-3002(63)91022-9","url":null,"abstract":"<div><p><em>Clostridium saccharobutyricum</em> extracts, heat treated at 65° have somewhat similar properties to iron-deficient extracts prepared from this organism: they cannot degrade pyruvate by the phosphoroclastic pathway or incorporate <sup>14</sup>CO<sub>2</sub> into pyruvate. However, they stimulate the clastic activity of normal extracts and restore the clastic activity of aged extracts. A mixture of heat-treated (65°) and iron-deficient extracts is inactive. The heat-treated (65°) extract has no stimulating effect on the <sup>14</sup>CO<sub>2</sub>-pyruvate exchange reaction. A cofactor FCL, of the formylfolic acid type was isolated from at 65° treated extracts. It increases the rat off oxidation of pyruvate. <em>N</em><sup>10</sup>-formyltetrahydrofolic acid replaces FCL whereas folic, <em>N</em><sup>10</sup>-formylfolic and <em>N</em><sup>5</sup>-formyltetrahydrofolic acids are inactive.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 569-576"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91022-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673330","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":"Quelques données sur la composition chimique des parois de Candida utilis","authors":"M. Novaes, J.R. Villanueva","doi":"10.1016/0006-3002(63)91066-7","DOIUrl":"https://doi.org/10.1016/0006-3002(63)91066-7","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 797-799"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91066-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92110950","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 conversion of retinyl methyl ether (vitamin A methyl ether) to retinol (vitamin A alcohol) in vivo","authors":"J.N. Thompson, G.A.J. Pitt","doi":"10.1016/0006-3002(63)91049-7","DOIUrl":"10.1016/0006-3002(63)91049-7","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 753-755"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91049-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673146","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":"Sodium compartmentation in turtle bladder","authors":"Clair M. Paine , E.C. Foulkes","doi":"10.1016/0006-3002(63)91054-0","DOIUrl":"10.1016/0006-3002(63)91054-0","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 767-768"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91054-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673151","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":"Abnormal human hemoglobins IX. Chemistry of hemoglobin JBaltimore","authors":"Corrado Baglioni , David J. Weatherall","doi":"10.1016/0006-3002(63)91029-1","DOIUrl":"10.1016/0006-3002(63)91029-1","url":null,"abstract":"<div><p>A human abnormal hemoglobin with the electrophoretic mobility of hemoglobin J has been isolated and studied. The amino acid substitution in this abnormal hemoglobin has been investigated. It has been found that an aspartic acid residue substitutes in this hemoglobin J the glycine residue present in position 16 of the β peptide chain. There are reasons to believe that the hemoglobin J studied is different from other hemoglobin J's. Accordingly, the hemoglobin studied has been specifically designated hemoglobin J<sub>Baltimore</sub>.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 637-643"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91029-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23676018","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 control of respiration in brain slices","authors":"Shigeki Minakami, Katsuko Kakinuma, Haruhisa Yoshikawa","doi":"10.1016/0006-3002(63)91070-9","DOIUrl":"10.1016/0006-3002(63)91070-9","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 808-811"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91070-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673168","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":"On the active site of myosin A-adenosine triphosphatase IV. Properties of binding of trinitrobenzenesulfonate and p-chloromercuribenzoate to myosin a","authors":"Yuji Tonomura , Junko Yoshimura, Toshiyuki Ohnishi","doi":"10.1016/0006-3002(63)91035-7","DOIUrl":"10.1016/0006-3002(63)91035-7","url":null,"abstract":"<div><p>The addition of ATP or PP<sub>i</sub> retarded conspicuously the rate of specific binding of trinitrobenzenesulfonate to one mole of lysine residue in 2.1·10<sup>5</sup> g of myosin A. The rate of specific binding of trinitrobenzenesulfonate to myosin A was increased in 4M LiBr which melts almost completely the helical structure of myosin A. The rate was also remarkably influenced by the treatment of myosin A with 1.5 M LiBr which inactivated ATPase (ATP phosphohydrolase, EC 3.6.1.3) without changing significantly the helical content of the myosin A molecule as a whole. Furthermore, it was demonstrated that actomyosin reconstituted from myosin A treated with <em>p</em>-chloromercuribenzoate and β-mercaptoethanol does not show a clearing response on addition of high concentrations of ATP and its ATPase activity is not inhibited by the substrate or by EDTA. The <em>p</em>-chloromercuribenzotae added was completely removed from myosin A by the further addition of excess β-mercaptoethanol and the optical rotatory dispersion of myosin A was insignificantly altered by the treatment with <em>p</em>-chloromercuribenzoate and β-mercaptoethanol.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 698-704"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91035-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673342","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}