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

{"title":"The effect of K+ on dephosphorylation of an acid stable phosphorylated intermediate of the (Na+-K+)-requiring ATPase activity","authors":"R. Rendi","doi":"10.1016/0926-6593(66)90187-1","DOIUrl":"10.1016/0926-6593(66)90187-1","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 394-396"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90187-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15336351","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 reaction of phosphages with ATP: Creatine phosphotransferase","authors":"Elizabeth James ,&nbsp;J.F. Morrison","doi":"10.1016/0926-6593(66)90179-2","DOIUrl":"https://doi.org/10.1016/0926-6593(66)90179-2","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A kinetic investigation has been made of the effect of various phosphagens on the reverse reaction catalysed by creatine kinase (ATP: creatine phosphotransferase, EC 2.7.3.2.).</p></span></li><li><span>2.</span><span><p>2. The results indicate that phosphoglycocyamine functions as a substrate of the enzyme with a maximum velocity only 0.18% of that obtained with phospho-creatine. Phosphotautocyamine and phosphoarginine were found not to act as substrates although they could combine with the enzyme as inhibitors.</p></span></li><li><span>3.</span><span><p>3. Values have been obtained for the tru kinetic constants associated with the reaction of each phosphagen with both the free enzyme and the enzyme-MgADP complex.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 327-336"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90179-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92150674","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":"Characteristics of the cysteinesulfinate-forming enzyme system in rat liver","authors":"Lena Ewetz,&nbsp;Bo Sörbo","doi":"10.1016/0926-6593(66)90176-7","DOIUrl":"10.1016/0926-6593(66)90176-7","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The oxidation of cysteine to cysteinesulfinate by rat-liver preparations in the presence of hydroxylamine has been studied. This compound is added to the assay system in order to inhibit the enzymatic destruction of the reaction product.</p></span></li><li><span>2.</span><span><p>2. The optimum assay conditions for the enzyme system are reported.</p></span></li><li><span>3.</span><span><p>3. The reaction is catalysed by a heat-labile factor found in the soluble fraction and is stimulated by TPNH, ferrous ions and mitochondria or microsomes. The stimulating activity in the particulate fractions is heat-labile.</p></span></li><li><span>4.</span><span><p>4. The enzyme system appears to be specific for <span>l</span>-cysteine, as very little sulfinate formation was detected when <span>d</span>-cysteine, <span>l</span>-cystine, glutathione or cysteamine was used as substrate.</p></span></li><li><span>5.</span><span><p>5. Among different rat tissues studied, only liver contained significant activity.</p></span></li><li><span>6.</span><span><p>6. The enzyme system is inhibited by heavy-metal reagents (EDTA, cyanide, <em>o</em>-phenanthroline) and by the sulfhydryl reagents <em>p</em>-hydroxymercuribenzoate and iodoacetate, but not by arsenite.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 296-305"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90176-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15489422","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":"Purification de la ribonucléase pancréatique de rat","authors":"A. Cozzone,&nbsp;G. Marchis-Mouren","doi":"10.1016/0926-6593(66)90188-3","DOIUrl":"10.1016/0926-6593(66)90188-3","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 396-399"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90188-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83208561","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":"Reaktionen von pyridinium oximen mit dem alkylphosphat dimethoat und seinen derivaten wirkung auf cholinesterasen","authors":"Ronald Zech,&nbsp;Hermann Engelhard,&nbsp;Wolf-Dietter Erdmann","doi":"10.1016/0926-6593(66)90183-4","DOIUrl":"10.1016/0926-6593(66)90183-4","url":null,"abstract":"<div><p><em>Reactions of pyridinium oximes with the alkyl phosphate dimethoate and its derivatives. Effects upon cholinesterases</em></p><ul><li><span>1.</span><span><p>1. Dimethoate (Rogor), a dimethoxydithioalkyl phosphate, does not inhibit the enzymes acetylcholinesterase (EC 3.1.1.7) and cholinesterase (EC 3.1.1.8). An isomerization product (the dithiol derivative) and an oxidation product (the O analogue) may be responsible for observed inhibitory effects. These derivatives are relatively weak inhibitors of cholinesterases.</p></span></li><li><span>2.</span><span><p>2. An attempt was made to reactivate the cholinesterases inhibited by these dimethoate derivatives. All the pyridinium oximes employed produced a stronger inhibition of the enzymes, if the concentrations of alkyl phosphate and oxime were high enough.</p></span></li><li><span>3.</span><span><p>3. A reaction scheme with a possible explanation for these effects is discussed.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 363-371"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90183-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75803843","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":"Activation of rat-liver microsomal glucose 6-phosphatase, inorganic pyrophosphatase and inorganic pyrophosphate-glucose phosphotransferase by hydroxyl ion","authors":"Marjorie R. Stetten,&nbsp;Foster F. Burnett","doi":"10.1016/0926-6593(66)90181-0","DOIUrl":"10.1016/0926-6593(66)90181-0","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. OH- has been shown to produce a 2- to 3-fold increase in the apparent activity <em>in vitro</em> of rat-liver microsomal glucose 6-phosphatase (EC 3.1.3.9) and the related enzymatic activities, inorganic pyrophosphatase, inorganic pyrophosphate-glucose phosphotransferase and adenosine-5′-triphosphate-glucose phosphotransferase.</p></span></li><li><span>2.</span><span><p>2. Optimal activation is achieved by pre-treatment of liver microsomes with ammonium or amino acid buffers at pH 9.5–9.8. Inactivation is observed above pH 10.</p></span></li><li><span>3.</span><span><p>3. This activation is as great or greater than that produced by deoxycholate or Triton X-100 treatment and the thermal instability introduced by these reagents is avoided.</p></span></li><li><span>4.</span><span><p>4. Alteration of the microsomal membranes by treatment with base is accompanied by a decrease in turbidity but does not result in a solubilization of the enzyme. The essential protein-lipid binding is apparently retained and the enzyme, so treated, is relatively stable at 30°.</p></span></li><li><span>5.</span><span><p>5. NH₄OH pretreatment of microsomes results in a lowering of the apparent Michaelis constant for glucose 6-phosphatase, similar to that caused by digitonin, deoxycholate and Triton X-100.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 344-350"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90181-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15397351","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":"Biphasic effects of nucleotides on potassium-dependent phosphatase","authors":"K. Nagai,&nbsp;H. Yoshida","doi":"10.1016/0926-6593(66)90193-7","DOIUrl":"10.1016/0926-6593(66)90193-7","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 410-412"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90193-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15397353","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 a peroxidase purified from beef thyroid tissues","authors":"Cecil C. Yip","doi":"10.1016/0926-6593(66)90173-1","DOIUrl":"10.1016/0926-6593(66)90173-1","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A peroxidase was purified from beef thyroid tissues by column chromatography on ion-exchange CM-Sephadex. Some of the properties of the purified enzyme were studied.</p></span></li><li><span>2.</span><span><p>2. By means of electrophoresis on polyacetate strips the purified enzyme was found to consist of one protein component. This single component demonstrated peroxidase activity when stained with <em>o</em>-dianisidine in the presence of H₂O₂.</p></span></li><li><span>3.</span><span><p>3. The molecular weight of the beef thyroid peroxidase was estimated to be approx. 50 000 by sucrose gradient centrifugation using as a reference a purified preparation of dog myeloperoxidase.</p></span></li><li><span>4.</span><span><p>4. Protoporphyrin IX was identified as the prosthetic group by spectral analysis of the acid methylethyl ketone extract and the pyridine haemochrome of the enzyme.</p></span></li><li><span>5.</span><span><p>5. Spectral properties of the enzyme complexes with CN- and CO, as well as its reduction by sodium dithionite, were distinctively different from those of bovine haemoglobin.</p></span></li><li><span>6.</span><span><p>6. Kinetic studies using <em>o</em>-dianisidine as a hydrogen donor showed that the <em>K</em>_<em>m</em> of the enzyme for H₂O₂ was between 1.5 to 2.0 · 10⁻⁵ M.</p></span></li><li><span>7.</span><span><p>7. The peroxidase activity of the enzyme was inhibited by SCN-, CN-, N₃-, F-, I-, propylthiouracil and Tapazole but not by <em>p</em>-hydroxymercuribenzoate or ClO₄- as shown by kinetic studies. Thyroid-stimulating hormone did not show any effect.</p></span></li><li><span>8.</span><span><p>8. The enzyme catalyzed also the iodination of tyrosine actively in the presence of added H₂O₂ or a H₂O₂-generating system. The iodination of tyrosine by this enzyme occurred optimally at pH 6. Thyroglobulin was iodinated much less actively.</p></span></li><li><span>9.</span><span><p>9. The enzymic iodination of tyrosine was inhibited by the inhibitors mentioned above, except iodide, and was not affected by thyroid-stimulating hormone.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 262-271"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90173-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043471","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 effects of pH on the rat liver tyrosine aminotransferase system","authors":"Gerald Litwack,&nbsp;Ilga Winicov,&nbsp;Joan M. Squires","doi":"10.1016/0926-6593(66)90191-3","DOIUrl":"10.1016/0926-6593(66)90191-3","url":null,"abstract":"","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 404-406"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90191-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17043483","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":"Transformations moleculaires au niveau des isozymes de la lacticodehydrogenase de la souris, mises en evidence par electrophorese en gel d'amidon","authors":"Jean-Francois Houssais","doi":"10.1016/0926-6593(66)90171-8","DOIUrl":"10.1016/0926-6593(66)90171-8","url":null,"abstract":"<div><p>Intra- and inter-isozymic molecular relationships of mouse lactate dehydrogenase (EC 1.1.1.27) have been studied using starch-gel electrophoresis. </p><ul><li><span>1.</span><span><p>1. Each isozyme (LDH 2 to LDH ₅) exhibits several narrow bands (sub-bands). These sub-bands present sequential and reversible molecular transformations inside the corresponding isozymic region of migration.</p></span></li><li><span>2.</span><span><p>2. Several physicochemical factors, <em>in vitro</em>, determine the direction of these molecular transformations.</p></span></li><li><span>3.</span><span><p>3. There are, in cells and tissues, definite specific properties, which are depending on the type of cellular differentiation, and which modify the behavior of the intra-isozymic sub-bands.</p></span></li><li><span>4.</span><span><p>4. The enzymatic form migrating towards the cathode (cathodic band) may release, under certain conditions, the isozymes LDH₅, LDH₄, LDH₃. This enzymatic form would appear to be an aggregation between isozymes. There is a relationship between cathodic band formation and the intra-isozymic sub-band transformations.</p></span></li></ul><p>A hypothesis according to which different molecular conformations of lactate dehydrogenase would account for these results, to a first approximation, is discussed.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 239-255"},"PeriodicalIF":0.0,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90171-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79278464","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}