Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects最新文献_第4页

Studies on the human prostatic acid phosphomonoesterase. Sulphhydryl and disulphide groups of the enzyme 人前列腺酸性磷酸单酯酶的研究。酶的巯基和二硫基

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90203-2

Jerzy Domański, Leszek Konieczny, Wo̵dzimierz Ostrowski

引用次数: 6

Isolation and properties of glutamine cyclotransferase of dried papaya latex 干木瓜胶乳谷氨酰胺环转移酶的分离及性质研究

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90204-4

M. Messer , M. Ottesen

引用次数: 55

Nouvelles recherches sur le chymotrypsinogène B evaluation quantitative dans le pancréas de boeuf et essai d'identification chez le porc 牛胰腺凝乳蛋白酶原B定量评价及猪胰腺鉴定试验的新研究

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90189-0

M Charles

{"title":"Nouvelles recherches sur le chymotrypsinogène B evaluation quantitative dans le pancréas de boeuf et essai d'identification chez le porc","authors":"M Charles","doi":"10.1016/0926-6569(64)90189-0","DOIUrl":"10.1016/0926-6569(64)90189-0","url":null,"abstract":"<div>In this work, bovine chymotrypsinogen B has been quantitatively determined and a first attempt has been made towards the identification of a chymotrypsinogen B in porcine pancreas.The quantitative technique used for bovine chymotrypsinogen B involves acid denaturation of procarboxypeptidase A, separation of anionic from cationic proteins on CM-cellulose at pH 6.0 and determination of the activity of both fractions against acetyl-l-tyrosine ethylester after tryptic activation. By using the specific activity of the pure precursors, the weight ratio chymotrypsinogen A/chymotrypsinogen B is finally calculated. This ratio is shown to be about 4 in bovine pancreas and pancreatic juice.The anionic proteins of porcine pancreas and pancreatic juice delay, as in the case of bovine pancreas a strong activity against acetyl-l-tyrosine ethylester. This kind of activity is not given by porcine procarboxypeptidase A which, in contrast with its bovine analog, does not hydrolyze acetyl-l-tyrosine ethylester after tryptic treatment, but my several other anionic proteins which can be partly separated on DEAE-cellulose at pH 8.0. It is not yet known whether or not one of these proteins is actually a chymotrypsinogen B.</div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 319-327"},"PeriodicalIF":0.0,"publicationDate":"1964-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90189-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75297302","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

Circular dichroism of aspartate transaminase 天冬氨酸转氨酶的环状二色性

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90197-X

Yu.N. Breusov, V.I. Ivanov, M.Ya. Karpeisky, Yu.V. Morozov

引用次数: 17

Asparate dehydrogenase activity of malate dehydrogenase 苹果酸脱氢酶的活性

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90200-7

Charles R. Shaw, Ann L. Koen

引用次数: 13

Activation of chymotrypsinogen B 凝乳胰蛋白酶原B的活化

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90188-9

Arlene Krehbiel , Beatrice Kassell, M. Laskowski Sr.

引用次数: 4

Pseudomonas aeruginosa peptide peptidohydrolase IV. Optical rotatory dispersion and amino acid composition 铜绿假单胞菌肽肽水解酶IV.旋光色散和氨基酸组成

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90194-4

Kazuyuki Morihara, Nobuo Yoshida, Kaoru Kuriyama

引用次数: 11

Purification and properties of malate dehydrogenase (Decarboxylating) from mycobacterium 607 607分枝杆菌苹果酸脱氢酶的纯化及性能研究

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90184-1

R. Parvin, S.V. Pande, T.A. Venkitasubramanian

{"title":"Purification and properties of malate dehydrogenase (Decarboxylating) from mycobacterium 607","authors":"R. Parvin, S.V. Pande, T.A. Venkitasubramanian","doi":"10.1016/0926-6569(64)90184-1","DOIUrl":"10.1016/0926-6569(64)90184-1","url":null,"abstract":"<div>Malate dehydrogenase (decarboxylating) (l-malate: NADP oxidoreductase (decarboxylating), EC 1.1.1.40) has been purified 100-fold from Mycobacterium 607, and its properties for oxidative decarboxylation reaction have been studied. The pH optimum was 7.8. Below pH 5.5 the enzyme was unstable. Reaction with NAD was slow. K3 for NADP was 4·10−5 M.Bivalent cations such as Mn2+, Mg2+, Co2+ or Ni2+ were essential for activity. The order and extent of effectiveness of these cations depended on the concentration of malate and Ks+. K+ activated the reaction, but higher substrate concentrations reduced or inhibitory. This inhibition was reversed completely by GSH and partially by increasing the activity bivalent cation concentration. The involvement of a sulfhydryl group in the enzymic reactions is also suggested by other inhibition studies.The apparent Ks for malate at pH 7.4 was 1☆10−3 M and at 8.2 it was 2.5·10−3 M. Higher malate concentrations were inhibitory. Raising the pH lowered, and increasing the Mg2+ concentration abolished, this effect. The cause of substrate inhibition is concluded to be its chelatioon of bivalent cation.Anions also affected the activity. Activity with Cl- was more than that with SO42− and this effect was more marled at higher pH.</div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 260-277"},"PeriodicalIF":0.0,"publicationDate":"1964-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90184-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23802404","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

Intracellular pH effect upon phosphoglucose isomerase in Escherichia coli 胞内pH值对大肠杆菌磷酸葡萄糖异构酶的影响

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90196-8

Leiv Klungsöyr

{"title":"Intracellular pH effect upon phosphoglucose isomerase in Escherichia coli","authors":"Leiv Klungsöyr","doi":"10.1016/0926-6569(64)90196-8","DOIUrl":"10.1016/0926-6569(64)90196-8","url":null,"abstract":"<div><ul><li>1.1. Whole cells of Escherichia coli hydrolyze fructose 1,6-diphosphate to fructose 6-phosphate, and when the cells are incubated in an unbuffered medium the product is not isomerized to glucose 6-phosphate. The reason for this lack of isomerization has been investigated.</li><li>2.Ubder specified conditions phosphoglucose isomerase (d-glucose-6-phosphate ketol isomerase, EC 5.3.1.9) is inhibited, probably because of a low pH in the cells which is unfavourable for the phosphoglucose isomerase reaction, but which permits other enzymes in the glycolytic sequence to act.</li><li>3.3. Aerobically incubated cells of E. coli contain more acids than what is found under anaerobic conditions. This may result in a pH inhibition of the phosphoglucose isomerase which is dependent upon the oxygen pressure.</li><li>4.4. In suspensions of E. coli buffered at pH 5.8, hydrolysis in the 1 position is competing favourably woth glycolytic breakdown of fructose 1,6-diphosphate.</li><li>5.5. The specific radioativity of mannitol 1-phosphate observed in experiments with 32P-labelled orthophosphate, strongly suggests that E. coli contains an active mannitol kinase.</li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 378-387"},"PeriodicalIF":0.0,"publicationDate":"1964-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90196-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82751309","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

Pseudomonas aeruginosa peptide peptidohydrolase

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-11-22 DOI: 10.1016/0926-6569(64)90193-2

Kazuyuki Morihasa, Hiroshige Tsuzuki

{"title":"Pseudomonas aeruginosa peptide peptidohydrolase","authors":"Kazuyuki Morihasa, Hiroshige Tsuzuki","doi":"10.1016/0926-6569(64)90193-2","DOIUrl":"10.1016/0926-6569(64)90193-2","url":null,"abstract":"<div>The twice recrystallized proteinase (peptide peptidohydrolase) of Pseudomonas aeruginosa IFO 3080 contained 1–2 gramatoms of Ca per mole (48 400 g) of enzyme protein and insignificant amounts of the other metal ions. Some chelating agents, such as ethylenediaminetetraacetic acid and o-phenanthroline, inhibited the enzymic activity, but the inactivation at 40° or below was easily reversed either by dialysis, dilution or the addition of various metal ions such as Zn2+, Co2+, Ca2+, etc. The Ca content of the enzyme protein was not decreased by the reversible inactivation, showing that the inactivation was produced by masking the Ca2+ of the enzyme with the chelating agent. To dissociate the Ca2+ from the enzyme protein, the inactivation treatment by chelating agent was made at 50°, but the trial was unsuccessful, that is, reactivation was no longer observed during the autodigestion of the enzyme protein. Thus the proteinase was regarded as a Ca2+-metalloenzyme, in which Ca2+ was tightly bound to the enzyme protein.</div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 351-360"},"PeriodicalIF":0.0,"publicationDate":"1964-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90193-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79813336","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: 24