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

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β-Fructofuranosidase from grape berries. III. The identity of the soluble and bound fractions 从葡萄浆果中提取的β-果糖呋喃苷酶。3。可溶分数和结合分数的同一性
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90160-3
Wilfred Niels Arnold
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引用次数: 7
Failure of certain inhibitors to prevent absorbance decreases of mitochondrial suspensions induced by hypotonicity and carbon tetrachloride 某些抑制剂不能防止低渗性和四氯化碳引起的线粒体悬液吸光度下降
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90155-X
Sasha Malamed, Jerry Weissman
{"title":"Failure of certain inhibitors to prevent absorbance decreases of mitochondrial suspensions induced by hypotonicity and carbon tetrachloride","authors":"Sasha Malamed, Jerry Weissman","doi":"10.1016/0926-6593(66)90155-X","DOIUrl":"10.1016/0926-6593(66)90155-X","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 181-183"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90155-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"16054064","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
β-Fructofuranosidase from grape berries II. Solubilization of a bound fraction 葡萄果实中的β-果糖呋喃苷酶结合分数的溶解
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90148-2
Wilfred Niels Arnold
{"title":"β-Fructofuranosidase from grape berries II. Solubilization of a bound fraction","authors":"Wilfred Niels Arnold","doi":"10.1016/0926-6593(66)90148-2","DOIUrl":"10.1016/0926-6593(66)90148-2","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A bound fraction of grabe <span><math><mtext>β-</mtext><mtext>fructofuranosidase</mtext></math></span> (EC 3.2.1.26) was solubilized by treatment with 0.2 M borate buffer (pH 8.5), whereas several other aqueous salts were without effect.</p></span></li><li><span>2.</span><span><p>2. In the system described, solubilization was influenced by boric acid concentration and pH but not by presentation time. Solubilization was essentially irreversible.</p></span></li><li><span>3.</span><span><p>3. Solubilization was maximal at pH 8.5; under more alkaline conditions, enzyme inactivation occurred. The decrease in amount of bound enzyme followed an inverse trend.</p></span></li><li><span>4.</span><span><p>4. Borate solubilization gave a total yield of <span><math><mtext>β-</mtext><mtext>fructofuranosidase</mtext></math></span> about 190% based on the starting material. This, together with the well-known interaction of borate with carbohydrates, suggested that a masking polysaccharide was operative in the starting material.</p></span></li><li><span>5.</span><span><p>5. The solubilized and soluble enzyme were partially purified and characterized. In both cases, only unsubstituted β-fructofuranosides were hydrolyzed. The Michaelis constants for sucrose were not significantly different.</p></span></li><li><span>6.</span><span><p>6. The dangers inherent in comparing the relative amounts of enzymes from different tissues were underlined by this experience.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 124-129"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90148-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043503","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: 22
Molecular forms of human-liver arginase 人肝精氨酸酶的分子形式
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90151-2
Luz Bascur, Julio Cabello, Marta Véliz, Adriana González
{"title":"Molecular forms of human-liver arginase","authors":"Luz Bascur,&nbsp;Julio Cabello,&nbsp;Marta Véliz,&nbsp;Adriana González","doi":"10.1016/0926-6593(66)90151-2","DOIUrl":"10.1016/0926-6593(66)90151-2","url":null,"abstract":"<div><p>The chromatography of liver homogenates and purified preparations of human-liver arginase (<span>l</span>-arginine ureohydrolase, EC 3.5.3.1) on CM-cellulose separates two protein fractions with arginase activity. On rechromatography, each of these fractions appears homogeneous and retains its adsorption-elution characteristics.</p><p>Both arginase fractions have similar properties as far as their affinities for substrates, pH optima and thermal inactivation are concerned. However, they differ in their pH stabilities and in their inhibition by ornithine and canavanine.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 149-154"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90151-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043506","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: 36
Uncoupling effect of amino compounds on choline oxidation in vitro 氨基化合物解偶联对胆碱体外氧化的影响
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90157-3
Kenneth T.N. Yue, Percy J. Russell, Dwight J. Mulford
{"title":"Uncoupling effect of amino compounds on choline oxidation in vitro","authors":"Kenneth T.N. Yue,&nbsp;Percy J. Russell,&nbsp;Dwight J. Mulford","doi":"10.1016/0926-6593(66)90157-3","DOIUrl":"10.1016/0926-6593(66)90157-3","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 187-189"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90157-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043510","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: 2
Comparative reduction of nitrate by spinach nitrate reductase with NADH2 and NADPH2 菠菜硝酸盐还原酶与NADH2和NADPH2还原硝酸盐的比较
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90162-7
A. Paneque, M. Losada
{"title":"Comparative reduction of nitrate by spinach nitrate reductase with NADH2 and NADPH2","authors":"A. Paneque,&nbsp;M. Losada","doi":"10.1016/0926-6593(66)90162-7","DOIUrl":"10.1016/0926-6593(66)90162-7","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 202-204"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90162-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15489104","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: 38
Analysis of 3α- and 3β-hydroxysteroid oxidoreductases of rat liver by disc electrophoresis 圆盘电泳法分析大鼠肝脏3α-和3β-羟基类固醇氧化还原酶
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90164-0
Elvira Doman, Samuel S. Koide
{"title":"Analysis of 3α- and 3β-hydroxysteroid oxidoreductases of rat liver by disc electrophoresis","authors":"Elvira Doman,&nbsp;Samuel S. Koide","doi":"10.1016/0926-6593(66)90164-0","DOIUrl":"10.1016/0926-6593(66)90164-0","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 209-211"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90164-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15489105","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: 15
The side activities of d-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating) from rabbit muscle: NADH-X formation d-甘油醛-3-磷酸的副活性:NAD+氧化还原酶(磷酸化)从兔肌肉:NADH-X的形成
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90143-3
A.G. Hilvers, J.H.M. Weenen, K. Van Dam
{"title":"The side activities of d-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating) from rabbit muscle: NADH-X formation","authors":"A.G. Hilvers,&nbsp;J.H.M. Weenen,&nbsp;K. Van Dam","doi":"10.1016/0926-6593(66)90143-3","DOIUrl":"10.1016/0926-6593(66)90143-3","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The formation of NADH-X from NADH in the presence of glyceraldehyde phosphate dehydrogenase (EC 1.2.1.12) at low pH is observed not only in the presence of pyrophosphate, citrate or phosphate, but also in the presence of arsenate.</p></span></li><li><span>2.</span><span><p>2. Stimulation of NADH-X formation by acetyl phosphate is dependent on the presence of enzyme-bound NAD<sup>+</sup>; however, added NAD<sup>+</sup> is inhibitory.</p></span></li><li><span>3.</span><span><p>3. Inhibition of NADH-X formation by sulphydryl reagents is prevented by acetyl phosphate in the presence of pyrophosphate or citrate, but not in the presence of arsenate or phosphate.</p></span></li><li><span>4.</span><span><p>4. In the absence of other polyvalent anions, acetyl phosphate alone can stimulate the conversion of NADH into NADH-X at low pH.</p></span></li><li><span>5.</span><span><p>5. In the presence of acetyl phosphate, the relative rate of formation of NAD<sup>+</sup> and NADH-X from NADH is dependent on the pH and the anions present.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 74-81"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90143-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85750069","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: 13
Rapid oxidation of palmitate with concomitant phosphorylation of adenosine 5′-diphosphate by moth flight-muscle mitochondria 飞蛾飞行肌线粒体伴随5 ' -二磷酸腺苷磷酸化的棕榈酸酯的快速氧化
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90138-X
Edmund Stevenson
{"title":"Rapid oxidation of palmitate with concomitant phosphorylation of adenosine 5′-diphosphate by moth flight-muscle mitochondria","authors":"Edmund Stevenson","doi":"10.1016/0926-6593(66)90138-X","DOIUrl":"10.1016/0926-6593(66)90138-X","url":null,"abstract":"<div><p>A procedure is described for isolating mitochondria from the thoracic muscle of the southern armyworm moth, <em>Prodenia eridania</em>. These mitochondria are capable of very rapidly oxidizing palmitate with concomitant phosphorylation of adenosine 5′-diphosphate. There is an absolute requirement for adenosine 5′-diphosphate and inorganic phosphate, but added nicotinamide-adenine dinucleotide, nicotinamide-adenine dinucleotide phosphate and carnitine have no effect. Maximal rates of oxygen uptake are found when a high-energy phosphate trap and some protein are present.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 29-33"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90138-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043517","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: 14
Morphological changes in isolated rat-liver mitochondria during swelling and contraction 离体大鼠肝脏线粒体在肿胀和收缩过程中的形态变化
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI: 10.1016/0926-6593(66)90139-1
Paulina Wlodawer , Donald F. Parsons , G.R. Williams , Lech Wojtczak
{"title":"Morphological changes in isolated rat-liver mitochondria during swelling and contraction","authors":"Paulina Wlodawer ,&nbsp;Donald F. Parsons ,&nbsp;G.R. Williams ,&nbsp;Lech Wojtczak","doi":"10.1016/0926-6593(66)90139-1","DOIUrl":"10.1016/0926-6593(66)90139-1","url":null,"abstract":"<div><p>Morphological changes of rat-liver mitochondria brought about by swelling and ATP-induced contraction were studied by electron microscopy. The course of swelling is proposed to be as follows: Entering of water (and solutes) causes breakage of the outer membrane and formation of protrusion of the inner membrane. The distention of the inner membrane is accompanied by loss of density of the matrix and by disapperance and change of shape of the cristae, probably due to their unfolding and evagination. Both membranes seem to possess a limited ability to stretch.</p><p>Addition of ATP to mitochondria swollen in the presence of either orthophosphate, oleate and thyroxine gave rise to structures different from mitochondria before the onset of swelling. Restoration of the mitochondrial morphology was not observed. It is thought that the processes initiated by ATP are not a simple reversal of swelling.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 34-47"},"PeriodicalIF":0.0,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90139-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043518","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
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