Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91067-9
Geraldine M. Purcell, Marion I. Barnhart
{"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":null,"pages":null},"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91022-9
Colette Delavier-Klutchko
Clostridium saccharobutyricum 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 14CO2 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 14CO2-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. N10-formyltetrahydrofolic acid replaces FCL whereas folic, N10-formylfolic and N5-formyltetrahydrofolic acids are inactive.
{"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":null,"pages":null},"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91066-7
M. Novaes, J.R. Villanueva
{"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":null,"pages":null},"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91049-7
J.N. Thompson, G.A.J. Pitt
{"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":null,"pages":null},"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91054-0
Clair M. Paine , E.C. Foulkes
{"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":null,"pages":null},"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91058-8
Donald Feldman , Milton Brenner , Michele B. Fleisher
{"title":"Aldosterone and rat-kidney enzymes","authors":"Donald Feldman , Milton Brenner , Michele B. Fleisher","doi":"10.1016/0006-3002(63)91058-8","DOIUrl":"10.1016/0006-3002(63)91058-8","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":null,"pages":null},"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)91058-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673155","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 : 1963-12-13DOI: 10.1016/0006-3002(63)91029-1
Corrado Baglioni , David J. Weatherall
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 JBaltimore.
{"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":null,"pages":null},"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":null,"pages":null},"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}
The addition of ATP or PPi retarded conspicuously the rate of specific binding of trinitrobenzenesulfonate to one mole of lysine residue in 2.1·105 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 p-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 p-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 p-chloromercuribenzoate and β-mercaptoethanol.
增加ATP或PPi弱智明显的特定绑定trinitrobenzenesulfonate一摩尔的赖氨酸残基105年2.1·克肌凝蛋白A特定绑定的trinitrobenzenesulfonate肌凝蛋白的速度增加4 M LiBr几乎完全融化的螺旋结构肌凝蛋白A率也显著影响肌凝蛋白的治疗与1.5 LiBr灭活的腺苷三磷酸酶(ATP phosphohydrolase,EC 3.6.1.3)，而不显著改变整个肌球蛋白A分子的螺旋含量。此外，研究表明，肌球蛋白A经对氯汞苯甲酸盐和β-巯基乙醇处理后重组的肌动球蛋白对高浓度ATP没有清除反应，其ATP酶活性不受底物或EDTA的抑制。加入过量的β-巯基乙醇后，肌球蛋白A中加入的对氯环苯甲醚被完全去除，对氯环苯甲酯和β-巯基乙醇对肌球蛋白A的旋光性影响不显著。
{"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":null,"pages":null},"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}
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