Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation最新文献_第10页

Highly purified dihydrofolate reductase of calf thymus 小牛胸腺高纯度二氢叶酸还原酶

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90035-X

David M. Greenberg, Bui-Duy Tam, Eduard Jenny, Benjamin Payes

引用次数: 22

Reduction of cytochrome c by amine oxidase from Aspergillus niger 黑曲霉胺氧化酶对细胞色素c的还原作用

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90048-8

Saburo Muraoka , Akira Hoshika , Hidemasa Yamasaki , Hideaki Yamada , Osao Adachi

引用次数: 3

Allantoinases from bacterial, plant and animal sources I. Purification and enzymic properties 细菌、植物和动物来源的尿囊酶1 .纯化和酶的性质

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90040-3

G.D. Vogels, F. Trijbels, A. Uffink

{"title":"Allantoinases from bacterial, plant and animal sources I. Purification and enzymic properties","authors":"G.D. Vogels, F. Trijbels, A. Uffink","doi":"10.1016/0926-6593(66)90040-3","DOIUrl":"10.1016/0926-6593(66)90040-3","url":null,"abstract":"<div><ul><li>1.1. Allantoinases (allantoin amidohydrolase, EC 3.5.2.5) from Streptococcus allantoicus, Arthrobacter allantoicus, Escherichia coli, Pseudomonas fluorescens, Pseudomonas acidovorans, frog liver, goldfish liver, Phaseolus hysterinus and Glycine hispida were studied.</li><li>2.2. The enzymes were purified 2.5- to 37-fold by (NH4)2SO4 precipitation and DEAE-cellulose chromatography.</li><li>3.3. The pH optimum curve, Michaelis constant, activation energy, stability and specificity were determined and compared.</li><li>4.4. The enzymes from S. allantoicus, A. allantoicus and E. coli were aspecific; the others degraded (+)-allantoin 4–22 times faster than (−)-allantoin.</li><li>5.5. The allantoinases from Ph. hysterinus and G. hispida were activated by acid pretreatment below pH 5.4.</li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"122 3","pages":"Pages 482-496"},"PeriodicalIF":0.0,"publicationDate":"1966-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90040-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75277661","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: 46

Composition en acides amines de l'ATP: l-arginine phosphotransferase cristallisee atp的氨基酸组成:l-精氨酸结晶磷酸转移酶

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90038-5

E. Der Terrossian, R. Kassab, L.A. Pradel, Nguyen Van Thoai

引用次数: 41

Hétéroenzymes d'acide adénosine 5′-triphosphorique: L-arginine phosphotransférase 5 ' -三磷酸腺苷杂酶:l -精氨酸磷酸转移酶

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90049-X

N.V. Thoai , N.V. Thiem , G. Lacombe , J. Roche

引用次数: 19

Kinetic properties and mechanism of action of human heart lactate dehydrogenase and α-hydroxybutyrate dehydrogenase 人心脏乳酸脱氢酶和α-羟基丁酸脱氢酶的动力学性质及作用机制

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90046-4

Doris Balinsky

引用次数: 5

Orotidine-5′-phosphate decarboxylase from higher plants 高等植物的5 ' -磷酸欧罗替丁脱羧酶

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90044-0

John H. Wolcott, Cleon Ross

引用次数: 34

The iodination of tyrosine by myeloperoxidase and beef thyroids. The possible involvement of free radicals 髓过氧化物酶和牛肉甲状腺对酪氨酸的碘化作用。自由基的可能参与

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90033-6

Cecil C. Yip, Linda D. Hadley

{"title":"The iodination of tyrosine by myeloperoxidase and beef thyroids. The possible involvement of free radicals","authors":"Cecil C. Yip, Linda D. Hadley","doi":"10.1016/0926-6593(66)90033-6","DOIUrl":"10.1016/0926-6593(66)90033-6","url":null,"abstract":"<div><ul><li>1.1. The oxidation of sulfite, measured by the uptake of oxygen, was employed to detect the formation of free radicals in the iodination of tyrosine by myeloperoxidase in the presence of added H2O2.</li><li>2.2. The uptake of oxygen was dependent on sulfite, tyrosine and myeloperoxidase. Tyrosine could be replaced by monoiodotyrosine, diiodotyrosine, 4-hydroxy-3,5-diiodophenylacetic acid or 4-hydroxy-3,5-diiodobenzaldehyde but not by thyroglobulin, phenylacetic acid, phenylalanine or iodide. Iodide was inhibitory.</li><li>3.3. The oxidation of sulfite under these conditions was affected by pH and had an optimal range between pH 5 and 6.5.</li><li>4.4. Sulfite and bisulfite inhibited completely the iodination of tyrosine and of thyroglobulin by myeloperoxidase in the presence of added H2O2. Sulfate was without effect.</li><li>5.5. The iodination of tyrosine by myeloperoxidase in the presence of added H2O2 showed the same pH optimum as the oxidation of sulfite.</li><li>6.6. A concentrated solubilized preparation of beef thyroid tissues, which catalyzed the peroxidation of <math><mtext>o-</mtext><mtext>dianisidine</mtext></math> and the iodination of tyrosine, could not substitute effectively for myeloperoxidase in the oxidation of sulfite. However, the iodination of tyrosine by this enzyme preparation was inhibited by sulfite and bisulfite.</li><li>7.7. These results are discussed in relation to a free radical reaction mechanism involved in the synthesis of iodotyrosines by myeloperoxidase and by the beef thyroid preparation.</li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"122 3","pages":"Pages 406-412"},"PeriodicalIF":0.0,"publicationDate":"1966-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90033-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76149664","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: 18

Lipoyl dehydrogenase from Saccharomyces cerevisiae II. Kinetic and inhibitor studies 酿酒酵母菌的脂酰脱氢酶。动力学和抑制剂研究

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90036-1

A. Wren , V. Massey

引用次数: 10

The development of intestinal β-galactosidase and β-glucuronidase in the newborn 新生儿肠道β-半乳糖苷酶和β-葡萄糖醛酸酶的发育

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI: 10.1016/0926-6593(66)90050-6

David Yi-Yung Hsia

引用次数: 7