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Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation最新文献

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A comparison of changes in lactate dehydrogenase isoenzyme patterns of porcine, human and bovine milk during lactation periods 哺乳期间猪、人、牛乳汁乳酸脱氢酶同工酶谱变化的比较
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-12-14 DOI: 10.1016/0926-6593(66)90024-5
Bengt Kjellberg, Børje Karlsson
{"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":"128 3","pages":"Pages 589-590"},"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}
引用次数: 6
Das redoxpotential der glukoseoxydase aus Aspergillus niger (Nigerin) in abhängigkeit vom pH 检测尼日阿斯帕格洛斯(尼安德逊)乳糖氧化物的可再生性浓度，与pH有关
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-12-14 DOI: 10.1016/0926-6593(66)90011-7
M.J. Walter
{"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":"128 3","pages":"Pages 504-509"},"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}
引用次数: 1
Effect of various bivalent cations and chelating agents on oxidative decarboxylation of α-keto acids 各种二价阳离子和螯合剂对α-酮酸氧化脱羧的影响
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-12-14 DOI: 10.1016/0926-6593(66)90019-1
Taro Hayakawa, Masahiro Hirashima, Minoru Hamada, Masahiko Koike
{"title":"Effect of various bivalent cations and chelating agents on oxidative decarboxylation of α-keto acids","authors":"Taro Hayakawa,&nbsp;Masahiro Hirashima,&nbsp;Minoru Hamada,&nbsp;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":"128 3","pages":"Pages 574-576"},"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}
引用次数: 3
Biochimica et biophysica acta, Biochimica et biophysica acta、
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-12-14 DOI: 10.1016/0926-6593(66)90030-0
{"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":"128 3","pages":"Page 603"},"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}
引用次数: 0
Studies on kynurenate hydroxylase: requirement for iron and flavin nucleotide 犬尿酸羟化酶的研究:对铁和黄素核苷酸的需求
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-12-14 DOI: 10.1016/0926-6593(66)90014-2
Masataka Mori , Hiroshi Taniuchi , Yutaka Kojima , Osamu Hayaishi
{"title":"Studies on kynurenate hydroxylase: requirement for iron and flavin nucleotide","authors":"Masataka Mori ,&nbsp;Hiroshi Taniuchi ,&nbsp;Yutaka Kojima ,&nbsp;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":"128 3","pages":"Pages 535-546"},"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}
引用次数: 4
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli 大肠杆菌对苏氨酸敏感的同型丝氨酸脱氢酶和天冬氨酸激酶活性
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-12-14 DOI: 10.1016/0926-6593(66)90005-1
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,&nbsp;Gisèle Le Bras,&nbsp;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":"128 3","pages":"Pages 450-453"},"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}
引用次数: 21
Metabolit-induzierte inaktivierung von glutaminsynthetase aus Escherichia coli im zellfreien system 在无细胞系统中杂交的谷氨酸对谷氨酸无效
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-12-14 DOI: 10.1016/0926-6593(66)90016-6
Dieter Mecke, Karl Wulff, Helmut Holzer
{"title":"Metabolit-induzierte inaktivierung von glutaminsynthetase aus Escherichia coli im zellfreien system","authors":"Dieter Mecke,&nbsp;Karl Wulff,&nbsp;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":"128 3","pages":"Pages 559-567"},"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}
引用次数: 32
Dielectric constant and enzyme kinetics solvent effects on the esterolytic activity of trypsin 介电常数和酶动力学溶剂对胰蛋白酶酯分解活性的影响
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-12-14 DOI: 10.1016/0926-6593(66)90021-X
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,&nbsp;Yoloxóchitl Bustamante,&nbsp;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":"128 3","pages":"Pages 578-581"},"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}
引用次数: 4
Isolation and purification of an acid phosphatase from baker's yeast (Saccharomyces cerevisiae) 面包酵母酸性磷酸酶的分离纯化
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-11-15 DOI: 10.1016/0926-6593(66)90189-5
P. Boer, Elizabeth P. Steyn-Parvé
{"title":"Isolation and purification of an acid phosphatase from baker's yeast (Saccharomyces cerevisiae)","authors":"P. Boer,&nbsp;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":"128 2","pages":"Pages 400-402"},"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}
引用次数: 59
The oxidation of fatty acids combined with albumin by isolated rat-liver mitochondria in the presence of fluorocitrate 游离大鼠肝线粒体在氟柠檬酸存在下对脂肪酸与白蛋白结合的氧化作用
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-11-15 DOI: 10.1016/0926-6593(66)90169-X
P. Björntorp
{"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":"128 2","pages":"Pages 221-227"},"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}
引用次数: 5
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