Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90279-2
Gene D. Pynes, Ezzat S. Younathan
{"title":"The subcellular distribution of inorganic pyrophosphatase in pigeon pancreas","authors":"Gene D. Pynes, Ezzat S. Younathan","doi":"10.1016/0926-6569(64)90279-2","DOIUrl":"10.1016/0926-6569(64)90279-2","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 150-151"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90279-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795485","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90284-6
Carlo Gregolin, Paola Scalella
{"title":"Phosphorylation linked to oxidation of D(−) and L-lactate by respiring particles from yeast","authors":"Carlo Gregolin, Paola Scalella","doi":"10.1016/0926-6569(64)90284-6","DOIUrl":"10.1016/0926-6569(64)90284-6","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 163-165"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90284-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795490","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90287-1
N.H. Sloane
{"title":"Phosphoglucomutase: A model for active0site characterization II. Optical rotatory dispersion studies","authors":"N.H. Sloane","doi":"10.1016/0926-6569(64)90287-1","DOIUrl":"10.1016/0926-6569(64)90287-1","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 171-172"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90287-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795493","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90288-3
David F. Wilson , Tsoo E. King
{"title":"Reconstitution of respiratory chain enzyme systems. XV. Reconstitution of succinate oxidase using soluble succinate dehydrogenase and a “cyanide particle”","authors":"David F. Wilson , Tsoo E. King","doi":"10.1016/0926-6569(64)90288-3","DOIUrl":"10.1016/0926-6569(64)90288-3","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 173-175"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90288-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795494","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90262-7
H. De Robichon-Szulmajster, D. Corrivaux
The kinetic of synthesis of the first enzymes of the part of pathway common to threonine and methionine synthesis in Saccharomyces cerevisiae have been studied, under conditions of repression followed by depression. The results show that repression is established immediately and that enzyme synthesis continues at a constant rate, whereas derepression is established slowly and progressively.
These results are in agreement with the hypothesis of a rapid transformation of exogenous repressor (end-product amino acid) into “endogenous repressor”. The slow elimination of the latter is probably due to temporary maintenance of exogenous repressoe in the amino acid pool of the cells.
{"title":"Régulations métaboliques de la biosynthèse de la méthionine et de la thréonine chez Saccharomyces cerevisiae","authors":"H. De Robichon-Szulmajster, D. Corrivaux","doi":"10.1016/0926-6569(64)90262-7","DOIUrl":"10.1016/0926-6569(64)90262-7","url":null,"abstract":"<div><p>The kinetic of synthesis of the first enzymes of the part of pathway common to threonine and methionine synthesis in <em>Saccharomyces cerevisiae</em> have been studied, under conditions of repression followed by depression. The results show that repression is established immediately and that enzyme synthesis continues at a constant rate, whereas derepression is established slowly and progressively.</p><p>These results are in agreement with the hypothesis of a rapid transformation of exogenous repressor (end-product amino acid) into “endogenous repressor”. The slow elimination of the latter is probably due to temporary maintenance of exogenous repressoe in the amino acid pool of the cells.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 1-9"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90262-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"103798913","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90273-1
A. Dahlqvist, D.L. Thomson
The intracellular locus of sucrose hydrolysis in rat small-intestinal mucosa has been studied in vitro using intestinal slices and homogenates of intestinal cells. The pH-activity curves for the invertase of the slices and homogenates were identical. The apparent Km for the invertase activity of the slices was considerably higher than the Km for the homogenates. The maximum velocity (V) for the slices and homogenates was nearly identical. Because of the difference in the apparent Km values, it is postulated that a barrier exists between the apical surface of the cell and the site of hydrolysis of sucrose by invertase. Since the barrier slows the transport of sucrose to the enzyme in the intact cells but permits rapid pH equilibration between the enzyme locus and the fluid bathing and brush border, the barrier may be located superficially.
{"title":"The hydrolysis of sucrose by intact and homogenized cells of rat small intestine. Influence of pH and substrate concentration","authors":"A. Dahlqvist, D.L. Thomson","doi":"10.1016/0926-6569(64)90273-1","DOIUrl":"10.1016/0926-6569(64)90273-1","url":null,"abstract":"<div><p>The intracellular locus of sucrose hydrolysis in rat small-intestinal mucosa has been studied <em>in vitro</em> using intestinal slices and homogenates of intestinal cells. The pH-activity curves for the invertase of the slices and homogenates were identical. The apparent <em>K</em><sub>m</sub> for the invertase activity of the slices was considerably higher than the <em>K</em><sub>m</sub> for the homogenates. The maximum velocity (<em>V</em>) for the slices and homogenates was nearly identical. Because of the difference in the apparent <em>K</em><sub>m</sub> values, it is postulated that a barrier exists between the apical surface of the cell and the site of hydrolysis of sucrose by invertase. Since the barrier slows the transport of sucrose to the enzyme in the intact cells but permits rapid pH equilibration between the enzyme locus and the fluid bathing and brush border, the barrier may be located superficially.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 99-104"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90273-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23793361","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90276-7
Glaci T. Zancan, Eduardo F. Recondo, Luis F. Leloir
An enzyme from muscle which acts on adenosine diphosphate phosphoglyceric acid and leads to the hydrolysis of the phosphate group at the 2-position of the glyceric acid moiety has been studied. The enzyme is strongly stimulated by inorgamoc pyrophosphate. This action is very specific. The enzyme also acts on 2,3-diphosphoglycerate.
{"title":"Enzymid dephosphorylation of adenosine diphosphate phosphoglyceric acid","authors":"Glaci T. Zancan, Eduardo F. Recondo, Luis F. Leloir","doi":"10.1016/0926-6569(64)90276-7","DOIUrl":"10.1016/0926-6569(64)90276-7","url":null,"abstract":"<div><p>An enzyme from muscle which acts on adenosine diphosphate phosphoglyceric acid and leads to the hydrolysis of the phosphate group at the 2-position of the glyceric acid moiety has been studied. The enzyme is strongly stimulated by inorgamoc pyrophosphate. This action is very specific. The enzyme also acts on 2,3-diphosphoglycerate.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 125-131"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90276-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795482","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90293-7
P. Feigelson
{"title":"On the role of free radicals in tryptophan pyrrolase catalysis","authors":"P. Feigelson","doi":"10.1016/0926-6569(64)90293-7","DOIUrl":"10.1016/0926-6569(64)90293-7","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 187-190"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90293-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23795499","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90270-6
Lorentz Engström
1.
1. A highly purified preparation of bovine-liver alkaline phosphatase (ortho-phosphoric monoester phosphohydrolase, EC 3.I.3.I) has been obtained from a liver homogenate treated with butanol. Acetone and ethanol fractionation have been used, followed by two consecutive chromatographies on TEAE-cellulose and one on Sephadex G-200.
2.
2. Labelled phosphorylserine has been isolated from acid hydrolysates of the purified enzyme, which had been incubated with radioactive orthophosphate and then inactivated by acid. Most probably, the phosphate was bound to a particular serine molecule at the active site of the enzyme. This supports the view that an intermediate phosphorylenzyme is formed during the action of alkaline phosphatase.
{"title":"Studies on bovine-liver alkaline phosphatase, purification, phosphate incorporation","authors":"Lorentz Engström","doi":"10.1016/0926-6569(64)90270-6","DOIUrl":"10.1016/0926-6569(64)90270-6","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A highly purified preparation of bovine-liver alkaline phosphatase (ortho-phosphoric monoester phosphohydrolase, EC 3.I.3.I) has been obtained from a liver homogenate treated with butanol. Acetone and ethanol fractionation have been used, followed by two consecutive chromatographies on TEAE-cellulose and one on Sephadex G-200.</p></span></li><li><span>2.</span><span><p>2. Labelled phosphorylserine has been isolated from acid hydrolysates of the purified enzyme, which had been incubated with radioactive orthophosphate and then inactivated by acid. Most probably, the phosphate was bound to a particular serine molecule at the active site of the enzyme. This supports the view that an intermediate phosphorylenzyme is formed during the action of alkaline phosphatase.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 71-78"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90270-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77550716","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}
Pub Date : 1964-10-23DOI: 10.1016/0926-6569(64)90298-6
Ronald E. Hurlbert, William B. Jakoby
{"title":"Reversible dissociation of l-tartaric acid dehydrase into subunits","authors":"Ronald E. Hurlbert, William B. Jakoby","doi":"10.1016/0926-6569(64)90298-6","DOIUrl":"10.1016/0926-6569(64)90298-6","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 202-204"},"PeriodicalIF":0.0,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90298-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23793352","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}
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