{"title":"Le role l'acide ascorbique dans l'oxydation enzymatique du diphosphopyridine nucléotide réduit","authors":"Etienne Gero","doi":"10.1016/0926-6569(64)90283-4","DOIUrl":"10.1016/0926-6569(64)90283-4","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 160-163"},"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)90283-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88464981","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":"Purification and characterization of ribonuclease from rabbit reticulocytes","authors":"Kenji Adachi, Kei Nagano, Toshiko Nakao, Makoto Nakao","doi":"10.1016/0926-6569(64)90269-X","DOIUrl":"10.1016/0926-6569(64)90269-X","url":null,"abstract":"<div><p>A method is described for the purification of ribonmuclease (EC 2.7.7.16) from rabbit reticulocytes by heart treatment at pH 2.5 followed by chromatography on a carboxymethylcellulose column. The enzymei was purified 5000-fold, and was free from both acid and alkaline phosphatases (EC 3.I.3.2 and EC 3.I.3.I, respectively), non-specific phosphodiesterase (EC 3.I.4.I) and deoxyribonuclease (EC 3.I.4.5).</p><p>The enzyme had a pH optimum at 5.8. It was heat and acid stable and could be stored at —20° for I year without loss of activity. The products of hydrolysis of yeast ribonucleic acid by the enzyme were found to contain both 2′- and 3′-purine and pyrimide nucleotides,t he ratio of ratio of adenylic to cytidylic acid being approximately I:I. An incomplete digest of yeast ribonucleic acid by the enzyme was separated on a diethylaminoethyl-cellulose column and both mono- and oligonucleotide fractions were identified. Nucleoside 2′- and 3′-cyclic phosphates were hydrolyzed to their corresponding non-cyclic mononucleotides by the enzyme.</p><p>A possible physiological role of the enzyme is discussed on the basis of the following experiments: (I) degradation of rabbit reticulocyte ribosome by the enzyme; (2) chronological difference in its activity in rabbit reticulocytes; and (3) intracellular localization of the enzyme.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 59-70"},"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)90269-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23793357","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 metabolism of l-rhamnose in Escherichia coli","authors":"Yasuyuki Takagi , Hideo Sawada","doi":"10.1016/0926-6569(64)90264-0","DOIUrl":"10.1016/0926-6569(64)90264-0","url":null,"abstract":"<div><p>Extracts of <em>Escherichia coli</em>, prepared from cells grown on <span>l</span>-rhamnose, contained a <span>l</span>-rhamnulose kinase (ATP:<span>l</span>-rhamnulose <span>i</span>-phosphotransferase, EC 2.7.1.5) which has been purified about 13-fold. The enzyme appears to be an SH enzyme, which catalyzes the phosphorylation of <span>l</span>-rhamnulose in the presence of ATP and some divalent metal ions but seems not to reactive with other sugars. Analytical studies on the phosphorulated sugar suggest that the reaction product is <span>l</span>-rhamnulose <span>i</span>-phosphate.</p><p>Evidence is present which indicates that the first step in the fermentation of <span>l</span>-rhamnose is the conversion of the methylpentose to <span>l</span>-rhamnulose followed by a phosphorylation of the ketose.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 18-25"},"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)90264-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795500","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":"Luminescence properties of muramidase and reoxidized muramidase","authors":"Jorge E. Churchich","doi":"10.1016/0926-6569(64)90295-0","DOIUrl":"10.1016/0926-6569(64)90295-0","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 194-197"},"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)90295-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795502","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":"Structure primaire d'un inhibiteur pancréatique de la trypsine (inhibiteur de Kunitz et Northrop)","authors":"J. Chauvet, G. Nouvel, R. Archer","doi":"10.1016/0926-6569(64)90297-4","DOIUrl":"https://doi.org/10.1016/0926-6569(64)90297-4","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 200-201"},"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)90297-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137439543","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 metabolism of l-rhamnose in escherichia coli","authors":"Yasuyuki Takagi , Hideo Sawada","doi":"10.1016/0926-6569(64)90263-9","DOIUrl":"10.1016/0926-6569(64)90263-9","url":null,"abstract":"<div><p><span>l</span>-Rhamnose isomearse (<span>l</span>-rhamnose ketol-isomerase) has been purified about 50-fold from extracts of <em>Escherichia coli</em>. THe enzyme appears to be an SH enzyme, and catalyzes the reversible reaction <span>l</span>-rhamnose ⇆ <span>l</span>-rhamnulose. The enzyme was activated by the addition of manganous ions. At equilibrium about 60% of the total methylpentose was present as <span>l</span>-rhamnulose.</p><p>The enzyme was specific for <span>l</span>-rhamnose and <span>l</span>-rhamnulose; no other sugars were found to react.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 10-17"},"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)90263-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795480","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":"Purification and chemical characterization of alanine dehydrogenase of Bacillus subtilis","authors":"Akira Yoshida, Ernst Freese","doi":"10.1016/0926-6569(64)90266-4","DOIUrl":"10.1016/0926-6569(64)90266-4","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. <em>Bacillus subtilis</em> alanine dehydrogenase (<span>L</span>-alanine: NAD oxidoreductase (deaminating), EC<sub>1.4.1.1.</sub> has been purified by column chromatography using calcium phosphate gel, DEAE-Sephadex and Ecteola-cellulose; it has been obtained in crystalline form.</p></span></li><li><span>2.</span><span><p>2. The sedimentation pattern indicated a homogenous preparation. The sedimentation constant at infinite dilution was 8.8 S. The molecular weight estimated by the sedimentation equilibrium method was 228 000.</p></span></li><li><span>3.</span><span><p>3. Amino acid analysis gave the following ratios of amino acid residues: Asp, <sub>43</sub>; Thr, <sub>34</sub>; Ser, <sub>20</sub>; Glu, <sub>51</sub>; Pro, <sub>25</sub>; Gly, <sub>51</sub>; Ala, <sub>65</sub>; CySH, <sub>2</sub>; Val, <sub>49</sub>; Met, <sub>11</sub>; iLeu, <sub>28</sub>; Leu, <sub>42</sub>; Tyr, <sub>15</sub>; Phe, <sub>7</sub>; Try, <sub>1</sub>; Lys, <sub>28</sub>; His, <sub>9</sub>; Arg, <sub>14</sub>.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 33-43"},"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)90266-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23793354","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":"Régulations métaboliques de la biosynthèse de la méthionine et de la thréonine chez Saccharomyces cerevisiae","authors":"H. De Robichon-Szulmajster, D. Corrivaux","doi":"10.1016/0926-6569(64)90262-7","DOIUrl":"10.1016/0926-6569(64)90262-7","url":null,"abstract":"<div><p>The kinetic of synthesis of the first enzymes of the part of pathway common to threonine and methionine synthesis in <em>Saccharomyces cerevisiae</em> have been studied, under conditions of repression followed by depression. The results show that repression is established immediately and that enzyme synthesis continues at a constant rate, whereas derepression is established slowly and progressively.</p><p>These results are in agreement with the hypothesis of a rapid transformation of exogenous repressor (end-product amino acid) into “endogenous repressor”. The slow elimination of the latter is probably due to temporary maintenance of exogenous repressoe in the amino acid pool of the cells.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 1-9"},"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)90262-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"103798913","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":"Phosphoglucomutase: A model for active0site characterization II. Optical rotatory dispersion studies","authors":"N.H. Sloane","doi":"10.1016/0926-6569(64)90287-1","DOIUrl":"10.1016/0926-6569(64)90287-1","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 171-172"},"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)90287-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795493","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":"Reconstitution of respiratory chain enzyme systems. XV. Reconstitution of succinate oxidase using soluble succinate dehydrogenase and a “cyanide particle”","authors":"David F. Wilson , Tsoo E. King","doi":"10.1016/0926-6569(64)90288-3","DOIUrl":"10.1016/0926-6569(64)90288-3","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 173-175"},"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)90288-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795494","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}