{"title":"β-Fructofuranosidase from grape berries. III. The identity of the soluble and bound fractions","authors":"Wilfred Niels Arnold","doi":"10.1016/0926-6593(66)90160-3","DOIUrl":"10.1016/0926-6593(66)90160-3","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 196-198"},"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)90160-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043513","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":"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}
{"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}
Luz Bascur, Julio Cabello, Marta Véliz, Adriana González
{"title":"Molecular forms of human-liver arginase","authors":"Luz Bascur, Julio Cabello, Marta Véliz, 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}
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, Percy J. Russell, 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}
{"title":"Comparative reduction of nitrate by spinach nitrate reductase with NADH2 and NADPH2","authors":"A. Paneque, 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}
{"title":"Analysis of 3α- and 3β-hydroxysteroid oxidoreductases of rat liver by disc electrophoresis","authors":"Elvira Doman, 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}
{"title":"The side activities of d-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating) from rabbit muscle: NADH-X formation","authors":"A.G. Hilvers, J.H.M. Weenen, 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}
{"title":"Properties of the induced acid phosphatase and of the constitutive acid phosphatase of Euglena","authors":"A. Bennun, J.J. Blum","doi":"10.1016/0926-6593(66)90147-0","DOIUrl":"10.1016/0926-6593(66)90147-0","url":null,"abstract":"<div><p>The induced acid phosphatase (EC 3.1.3.2) of <em>Euglena gracilis</em> has been solubilized and partially purified. The enzyme has a wide range of substrate specificity and, as predicted from earlier studies on whole cells, the ratio of its activity at pH 5 to its activity at pH 7 in presence of 5 mM fluoride is 1.1 for <span><math><mtext>p-</mtext><mtext>nitrophenylphosphate</mtext></math></span> as substrate. The enzyme is competitively inhibited by arsenate and phosphate, but exhibits mixed competitive-non-competitive inhibition with molybdate. The enzyme migrates towards the cathode when electrophoresis is performed on cellulose acetate strips at pH 8.2. Euglena also contains several other acid phosphatases. The two major constitutive acid phosphatases, which remain particle-bound after a variety of extraction procedures, differ in their thermal stability from each other and from the induced phosphatase. The ratio of activity at pH 5 to the activity at pH 7 <em>plus</em> 5 mM fluoride for the mixture of these two constitutive enzymes is 15. These observations establish that the increase in acid phosphatase activity occurring in Euglena in response to phosphate deprivation is due to the synthesis of a separate enzyme. The heat of thermal inactivation of the purified induced enzyme is about four times larger than the heat of denaturation computed from the effect of temperature on the rate of reversion of the induced phosphatase <em>in vivo</em>.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 106-123"},"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)90147-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15399090","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":"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}