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

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The interaction of penicillinase with penicillins III. Comparison of exopenicillinase preparations of various origins 青霉酶与青霉素的相互作用III。不同产地外霉素酶制剂的比较
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90017-3
N. Citri, N. Garber, A. Kalkstein
{"title":"The interaction of penicillinase with penicillins III. Comparison of exopenicillinase preparations of various origins","authors":"N. Citri,&nbsp;N. Garber,&nbsp;A. Kalkstein","doi":"10.1016/0926-6569(64)90017-3","DOIUrl":"10.1016/0926-6569(64)90017-3","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The interaction of various penicillinases (penicillin amidohydrolase, EC 3.5.2.6) with methicillin and oxacillin has been studied.</p></span></li><li><span>2.</span><span><p>2. The <em>K</em><sub>m</sub> values have been compared and found to reflect the phylogenetic and serological relationship of the penicillinases.</p></span></li><li><span>3.</span><span><p>3. Methicillin and oxacillin accelerate the inactivation of penicillinases by heat and by urea, and expose groups sensitive to iodine and to <em>p</em>-chloromercuribenzoate (<em>p</em>-hydroxymercuribenzoate).</p></span></li><li><span>4.</span><span><p>4. The response of penicillinases from different sources to various concentrations of these analogs has been compared.</p></span></li><li><span>5.</span><span><p>5. The patterns of response are characteristic of the source of penicillinase, and essentially independent of the structure of the analog.</p></span></li><li><span>6.</span><span><p>6. A comparison of these patterns brings out subtle differences in the tertiary structure of the active sites of closely related enzymes.</p></span></li><li><span>7.</span><span><p>7. The sensitivity of such analysis is illustrated by the difference in reponse patterns of enzymically and serologically indistinguishable induced and constitutive enzyme preparations.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 572-581"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90017-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23815497","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
Electron transport in Peptostreptococcus elsdenii 埃氏胃链球菌的电子传递
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90001-X
R.L. Baldwin, L.P. Milligan
{"title":"Electron transport in Peptostreptococcus elsdenii","authors":"R.L. Baldwin,&nbsp;L.P. Milligan","doi":"10.1016/0926-6569(64)90001-X","DOIUrl":"10.1016/0926-6569(64)90001-X","url":null,"abstract":"<div><p>The electron-transfer reactions associated with acyl-CoA dehydrogenase (acyl-CoA: DPN<sup>+</sup> oxidoreductase), hydrogenase (EC 1.98.1.1) and lactic dehydrogenase (<span>dl</span>-lactate: (acceptor) oxidoreductase) in the rumen microorganism <em>Peptostreptococcus elsdenii</em> were studied and a pathway of electron transport in the organism proposed. Acyl-CoA dehydrogenase was resolved into dehydrogenase and an associated electron-transport protein (Fraction II) which accepts electrons from DPNH and passes them to the dehydrogenase. The two components were purified and partially characterized. Data indicating the presence of a ferredoxin-linked DPN<sup>+</sup> reductase (reduced ferredoxin: DPN<sup>+</sup> oxidoreductase) are presented.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 421-432"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90001-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23820184","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: 34
Bestimmung von transaminasen in gegenwart von glutamat-dehydrogenase 氨化酶中含有氨化酶
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90024-0
Christian Streffer
{"title":"Bestimmung von transaminasen in gegenwart von glutamat-dehydrogenase","authors":"Christian Streffer","doi":"10.1016/0926-6569(64)90024-0","DOIUrl":"10.1016/0926-6569(64)90024-0","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 612-615"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90024-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87815983","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: 3
The pyrophosphorylysis of adenosine diphosphate glucose and adenosine diphosphate mannose 二磷酸腺苷葡萄糖和二磷酸腺苷甘露糖的热磷酸化
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90008-2
H. Verachtert, S.T. Bass, R.G. Hansen
{"title":"The pyrophosphorylysis of adenosine diphosphate glucose and adenosine diphosphate mannose","authors":"H. Verachtert,&nbsp;S.T. Bass,&nbsp;R.G. Hansen","doi":"10.1016/0926-6569(64)90008-2","DOIUrl":"10.1016/0926-6569(64)90008-2","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The biosynthesis of adenosine diphosphate glucose and adenosine diphosphate mannose from adenosine triphosphate and respectively glucose 1-phosphate and mannose 1-phosphate has been observed in extracts from mammalian tissues. The reaction is reversible in the presence of the nucleoside diphosphate sugar and pyrophosphate.</p></span></li><li><span>2.</span><span><p>2. Two different enzymes are probably responsible for the reactions with either adenosine diphosphate glucose or adenosine diphosphate mannose.</p></span></li><li><span>3.</span><span><p>3. Adenosine diphosphate mannose may be synthesized by the same enzyme which catalyzes the biosynthesis of guanosine diphosphate mannose and inosine diphosphate mannose.</p></span></li><li><span>4.</span><span><p>4. Evidence is presented that adenosine diphosphate glucose pyrophosphorylase (ATP: α-<span>d</span>-glucose-1-phosphate adenylyltransferase) may be a specific enzyme.</p></span></li><li><span>5.</span><span><p>5. The relative levels of nucleoside diphosphate hexose pyrophosphorylases have been measured in different extracts from mammals, plants or yeast. From these data the possible significance of adenosine diphosphate glucose pyrophosphorylase in mammals is discussed.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 482-488"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90008-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23815488","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: 8
Shift of cytochrome oxidase α-peak from 603–605 mμ to 590 mμ by heat denaturation 热变性使细胞色素氧化酶a峰从603605 m移至590 m
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90021-5
Philip Person, Herbert Zipper
{"title":"Shift of cytochrome oxidase α-peak from 603–605 mμ to 590 mμ by heat denaturation","authors":"Philip Person,&nbsp;Herbert Zipper","doi":"10.1016/0926-6569(64)90021-5","DOIUrl":"10.1016/0926-6569(64)90021-5","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 605-607"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90021-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87982784","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
A procedure which demonstrates substrate inhibition of tyrosinase 一个证明底物抑制酪氨酸酶的程序
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90020-3
E.A. Kean
{"title":"A procedure which demonstrates substrate inhibition of tyrosinase","authors":"E.A. Kean","doi":"10.1016/0926-6569(64)90020-3","DOIUrl":"10.1016/0926-6569(64)90020-3","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 602-604"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90020-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23815312","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
A correlation between the protein structure and catalytic activity of aspartate aminotransferase 天冬氨酸转氨酶的蛋白质结构与催化活性的关系
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90030-6
Paolo Fasella , Gordon G. Hammes
{"title":"A correlation between the protein structure and catalytic activity of aspartate aminotransferase","authors":"Paolo Fasella ,&nbsp;Gordon G. Hammes","doi":"10.1016/0926-6569(64)90030-6","DOIUrl":"10.1016/0926-6569(64)90030-6","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 630-632"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90030-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23815320","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: 4
The effect of mutation on two forms of phosphoglucomutase in Saccharomyces 突变对酵母菌中两种形式磷酸葡萄糖糖脲酶的影响
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90011-2
Andrew Tsoi , H.C. Douglas
{"title":"The effect of mutation on two forms of phosphoglucomutase in Saccharomyces","authors":"Andrew Tsoi ,&nbsp;H.C. Douglas","doi":"10.1016/0926-6569(64)90011-2","DOIUrl":"10.1016/0926-6569(64)90011-2","url":null,"abstract":"<div><p>The Saccharomyces haploid stock 8050B is a galactose fermenter which was found by chromatography on CM-cellulose and electrophoresis on agar gel to contain a major and a minor form of phosphoglucomutase (<span>d</span>-glucose-1,6-diphosphate:<span>d</span>-glucose-1-phosphate phosphotransferase, EC 2.7.5.1). Mutations in the <em>Ga<sub>5</sub></em> locus of this stock reduced the phosphoglucomutase activity in extracts 4–5-fold and rendered the cells unable to ferment galactose. The reduction in enzyme activity of the mutants was shown to be due to the fact that the synthesis of the major phosphoglucomutase component was blocked, although the minor component was not affected. The two phosphoglucomutases are probably the products of different genes.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 513-520"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90011-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23815491","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: 18
Stability of nicotinamide - adenine dinucleotide phosphate and nicotinamide - adenine dinucleotide in tissue extracts under mildly acidic conditions 烟酰胺-腺嘌呤二核苷酸磷酸和烟酰胺-腺嘌呤二核苷酸在轻度酸性条件下组织提取物中的稳定性
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90023-9
Diether Neubert, Hans-Ulrich Schulz, Rainer Hoehne
{"title":"Stability of nicotinamide - adenine dinucleotide phosphate and nicotinamide - adenine dinucleotide in tissue extracts under mildly acidic conditions","authors":"Diether Neubert,&nbsp;Hans-Ulrich Schulz,&nbsp;Rainer Hoehne","doi":"10.1016/0926-6569(64)90023-9","DOIUrl":"10.1016/0926-6569(64)90023-9","url":null,"abstract":"","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 610-612"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90023-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23820187","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
Proteolytic enzymes of Penicillium janthinellum 青霉菌的蛋白水解酶。一种胰蛋白酶原活化酶(肽酶a)的纯化和性质。
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI: 10.1016/0926-6569(64)90014-8
T. Hofmann , R. Shaw
{"title":"Proteolytic enzymes of Penicillium janthinellum","authors":"T. Hofmann ,&nbsp;R. Shaw","doi":"10.1016/0926-6569(64)90014-8","DOIUrl":"10.1016/0926-6569(64)90014-8","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>(1) A trypsinogen-activating proteolytic enzyme (peptidase A) has been isolated from the growth medium of <em>Penicillium janthinellum</em> and purified about 60-fold; it is homogeneous in the ultra-centrifuge and on electrophoresis. Its molecular weight is 32 000.</p></span></li><li><span>2.</span><span><p>(2) The enzyme has the following amino acid composition: Lys<sub>5</sub>, His<sub>3</sub>, Asp<sub>36</sub>, Thr<sub>28</sub>, Ser<sub>42</sub>, Glu<sub>28</sub>, Pro<sub>12</sub>, Gly<sub>39</sub>, Ala<sub>23</sub>, Val<sub>22</sub>, Ileu<sub>12.5</sub>, Leu<sub>20</sub>, Tyr<sub>14</sub>, Phe<sub>19</sub>, Try<sub>4–5</sub>. It does not contain arginine, methione and half-crystine.</p></span></li><li><span>3.</span><span><p>(3) The system peptidase A-trypsinogen follows Michealis-Menten kinetics, giving <em>K</em><sub>m</sub> = (7.6±2) · 10<sup>−6</sup> M (at 0°, pH 3.4).</p></span></li><li><span>4.</span><span><p>(4) Peptidase A apparently does not act on small peptides, but readily degrades apoferritin and bovine serum albumin. About 15% of the peptide bonds in bovine serum albumin are hydrolysed.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 543-557"},"PeriodicalIF":0.0,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90014-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89055812","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: 47
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