{"title":"A comparison of changes in lactate dehydrogenase isoenzyme patterns of porcine, human and bovine milk during lactation periods","authors":"Bengt Kjellberg, Børje Karlsson","doi":"10.1016/0926-6593(66)90024-5","DOIUrl":"10.1016/0926-6593(66)90024-5","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90024-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88131229","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":"Das redoxpotential der glukoseoxydase aus Aspergillus niger (Nigerin) in abhängigkeit vom pH","authors":"M.J. Walter","doi":"10.1016/0926-6593(66)90011-7","DOIUrl":"10.1016/0926-6593(66)90011-7","url":null,"abstract":"<div><p>The oxidation-reduction potential of the glucose oxidase from <em>Aspergillus niger</em> was determined by titration with leucosafranine in the pH range 4.5–7.5. The results are compared with the oxidation-reduction potential values reported by K<span>e</span><sup>1</sup> for FAD. Possibilities for the binding between the apoprotein and the prosthetic group are discussed.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90011-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89191444","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 various bivalent cations and chelating agents on oxidative decarboxylation of α-keto acids","authors":"Taro Hayakawa, Masahiro Hirashima, Minoru Hamada, Masahiko Koike","doi":"10.1016/0926-6593(66)90019-1","DOIUrl":"10.1016/0926-6593(66)90019-1","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90019-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84249099","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":"Biochimica et biophysica acta,","authors":"","doi":"10.1016/0926-6593(66)90030-0","DOIUrl":"https://doi.org/10.1016/0926-6593(66)90030-0","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90030-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137408308","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Masataka Mori , Hiroshi Taniuchi , Yutaka Kojima , Osamu Hayaishi
{"title":"Studies on kynurenate hydroxylase: requirement for iron and flavin nucleotide","authors":"Masataka Mori , Hiroshi Taniuchi , Yutaka Kojima , Osamu Hayaishi","doi":"10.1016/0926-6593(66)90014-2","DOIUrl":"10.1016/0926-6593(66)90014-2","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Kynurenate hydroxylase (kynurenate, NAD(P)H:O<sub>2</sub> oxidoreductase (hydroxylating), EC 1.14.1.3), an enzyme which catalyzes the conversion of kynurenate to kynurenate-7,8-dihydrodiol, has been purified from Pseudomonas.</p></span></li><li><span>2.</span><span><p>2. The partially purified enzyme preparation is stimulated 6–8 fold by the addition of ferrous ion. It is strongly inhibited by <span><math><mtext>o-</mtext><mtext>phenanthroline</mtext></math></span> and α,α′-dipyridyl and its activity is specifically restored by the addition of ferrous ion.</p></span></li><li><span>3.</span><span><p>3. Flavin nucleotides were shown to participate in the kynurenate hydroxylase reaction. After acid ammonium sulfate treatment of the enzyme, it is active only upon the addition of flavin nucleotides.</p></span></li><li><span>4.</span><span><p>4. The enzyme is unstable but is fairly well protected from inactivation by some reducing agents, heated extracts, or in an atmosphere of nitrogen. The enzyme, once inactivated by oxygen, can be reactivated almost to the original level by the addition of sodium borohydride. The effects of various reducing agents and conditions required for this reactivation have been studied. required for this reactivation have been studied.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90014-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81925490","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}
Paolo Truffa-Bachi, Gisèle Le Bras, Georges N. Cohen
{"title":"The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli","authors":"Paolo Truffa-Bachi, Gisèle Le Bras, Georges N. Cohen","doi":"10.1016/0926-6593(66)90005-1","DOIUrl":"10.1016/0926-6593(66)90005-1","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Homoserine dehydrogenase I (<span>l</span>-homoserine:NADP<sup>+</sup> oxidoreductase, EC 1.1.1.3) of <em>Escherichia coli</em> is inactivated with apparent first-order kinetics by exposure at pH 9 in Tris buffer. This inactivation is accompanied by desensitization of the enzyme towards threonine.</p></span></li><li><span>2.</span><span><p>2. <span>L</span>-Aspartate and ATP, the substrates of the associated activity, β-aspartokinase I (ATP:<span>L</span>-aspartate 4-phosphotransferase, EC 2.7.2.4) protect against the desensitization of homoserine dehydrogenase.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90005-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86818248","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":"Metabolit-induzierte inaktivierung von glutaminsynthetase aus Escherichia coli im zellfreien system","authors":"Dieter Mecke, Karl Wulff, Helmut Holzer","doi":"10.1016/0926-6593(66)90016-6","DOIUrl":"10.1016/0926-6593(66)90016-6","url":null,"abstract":"<div><p>A system is described in which glutaminine synthetase (EC 6.3.1.2) from <em>Escherichia coli</em> B is irreversibly inactivated by incubation with ATP, Mg<sup>2+</sup> and gluatmine or glutamate <em>in vitro</em>. Under the conditions chose, the glutamyl transferase activity does not change significantly.</p><p>Mechanisms are discussed for the in activation of glutamine synthetase <em>in vitro</em> as well as the relationship of this process to the inactivation of the enzyme by NH<sub>4</sub><sup>+</sup> in intact cells.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90016-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83351176","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}
Luz Maria Del Castillo, Yoloxóchitl Bustamante, M. Castañeda-Agulló
{"title":"Dielectric constant and enzyme kinetics solvent effects on the esterolytic activity of trypsin","authors":"Luz Maria Del Castillo, Yoloxóchitl Bustamante, M. Castañeda-Agulló","doi":"10.1016/0926-6593(66)90021-X","DOIUrl":"10.1016/0926-6593(66)90021-X","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90021-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85471598","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":"Isolation and purification of an acid phosphatase from baker's yeast (Saccharomyces cerevisiae)","authors":"P. Boer, Elizabeth P. Steyn-Parvé","doi":"10.1016/0926-6593(66)90189-5","DOIUrl":"10.1016/0926-6593(66)90189-5","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90189-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043481","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 oxidation of fatty acids combined with albumin by isolated rat-liver mitochondria in the presence of fluorocitrate","authors":"P. Björntorp","doi":"10.1016/0926-6593(66)90169-X","DOIUrl":"10.1016/0926-6593(66)90169-X","url":null,"abstract":"<div><p>Fluorocitrate was investigated as an inhibitor of the citric acid cycle which could make possible the separate study of β-oxidation of fatty acids bound to albumin using isolated rat-liver mitochondria. Fluorocitrate was shown to inhibit completely not only the CO<sub>2</sub> formation but also the incorporation of label from fatty acids into citrate in agreement with previous work. The reaction products identified were acetoacetate and β-hydroxybutyrate. No evidence for interference of fluorocitrate with β-oxidation or with phosphorylation coupled to this oxidation was found. Acetoacetate formation from fatty acids was rapid and initially linear.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90169-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043469","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}