{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T19:37:51Z","timestamp":1761766671675},"reference-count":11,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[1968,1,1]],"date-time":"1968-01-01T00:00:00Z","timestamp":-63158400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[1968,1]]},"abstract":"<jats:p>\n            When grown autotrophically in a thiosulfate-mineral salts medium, cells of the facultative chemoautotrophic bacterium,\n            <jats:italic>Thiobacillus novellus<\/jats:italic>\n            , produced two distinct glutamate dehydrogenases, one specific for nicotinamide adenine dinucleotide phosphate (NADP) and the other specific for nicotinamide adenine dinucleotide (NAD). When glutamate was supplied exogenously as the sole carbon source, the NAD-specific glutamate dehydrogenase was fully induced. Lower levels of the enzyme were found in bacteria grown in\n            <jats:sc>l<\/jats:sc>\n            -arginine,\n            <jats:sc>l<\/jats:sc>\n            -alanine, glucose, glycerol, lactate, citrate, or succinate. Arginine, histidine, and aspartate, on the other hand, caused a marked repression of the NADP-specific glutamate dehydrogenase activity. The NAD-dependent glutamate dehydrogenase was allosteric. Adenosine-5\u2032-monophosphate and adenosine-5\u2032-diphosphate acted as positive effectors. Both glutamate dehydrogenases were purified about 250-fold and were shown to be distinct protein with different physical properties.\n          <\/jats:p>","DOI":"10.1128\/jb.95.1.87-94.1968","type":"journal-article","created":{"date-parts":[[2020,1,5]],"date-time":"2020-01-05T02:04:46Z","timestamp":1578189886000},"page":"87-94","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":39,"title":["Evidence for Two Species of Glutamate Dehydrogenases in\n            <i>Thiobacillus novellus<\/i>"],"prefix":"10.1128","volume":"95","author":[{"given":"H. B.","family":"L\u00e9John","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg 19, Manitoba, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Barbara-Ellen","family":"McCrea","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg 19, Manitoba, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"p_1","first-page":"2682","article-title":"Kinetics of regulatory enzymes. Kinetic order of the yeast diphosphopyridine nucleotide isocitrate dehydrogenase reaction and a model for the reaction","volume":"240","author":"ATKINSON D. E.","year":"1965","unstructured":"ATKINSON , D. E. , J. A. HATHAWAY , A ND E . C. SMITH. 1965 . Kinetics of regulatory enzymes. Kinetic order of the yeast diphosphopyridine nucleotide isocitrate dehydrogenase reaction and a model for the reaction . J. Biol. Chem. 240 : 2682 - 2690 .","journal-title":"J. Biol. Chem."},{"key":"p_2","unstructured":"BERGMEYER H.-U. AND E. BERNT. 1963. Glutamate-oxaloacetate transaminase p. 384-388. In H.-U. Bergmeyer [ed.] Methods of enzymatic analysis. Academic Press Inc. New York."},{"key":"p_3","first-page":"2028","article-title":"Glutamate dehydrogenase. VI. Survey of purine nucleotide and other effects on the enzyme from various sources","volume":"240","author":"FRIEDEN C.","year":"1965","unstructured":"FRIEDEN , C. 1965 . Glutamate dehydrogenase. VI. Survey of purine nucleotide and other effects on the enzyme from various sources . J. Biol. Chem. 240 : 2028 - 2035 .","journal-title":"J. Biol. Chem."},{"key":"p_4","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1073\/pnas.42.8.481","article-title":"Phosphorylative and non-phosphorylative pathways of electron transfer in rat liver mitochondria","author":"KAPLAN N. P.","year":"1956","unstructured":"KAPLAN , N. P. , M. N. SWARTZ , M. E. FRECH , A ND M . M. Cio TT i. 1956 . Phosphorylative and non-phosphorylative pathways of electron transfer in rat liver mitochondria . Proc. Natl. Acad. Sci. U. S. 42: 481 - 487 .","journal-title":"Proc. Natl. Acad. Sci. U."},{"key":"p_5","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1128\/BR.27.2.155-169.1963","article-title":"Multiple forms of enzymes","volume":"27","author":"KAPLAN N.","year":"1963","unstructured":"KAPLAN , N. 0. , 1963 . Multiple forms of enzymes . Bacteriol. Rev. 27 : 155 - 169 .","journal-title":"Bacteriol. Rev."},{"key":"p_6","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/0006-291X(67)90412-3","article-title":"AMP-activation of an allosteric NAD-dependent glutamate dehydrogenase","volume":"28","author":"JOHN H. B.","year":"1967","unstructured":"L1 JOHN , H. B. 1967 . AMP-activation of an allosteric NAD-dependent glutamate dehydrogenase . Biochem. Biophys. Res. Commun. 28 : 96 - 102 .","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"p_7","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1128\/JB.94.5.1484-1491.1967","article-title":"Catabolite repression in the facultative chemoautotroph Thiobacillus novellus","volume":"94","author":"JOHN H. B.","year":"1967","unstructured":"Li JOHN , H. B. , L. VAN CAESEELE , A ND H . LEE s. 1967 . Catabolite repression in the facultative chemoautotroph Thiobacillus novellus . J. Bacteriol. 94 : 1484 - 1491 .","journal-title":"J. Bacteriol."},{"key":"p_8","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","article-title":"Protein measurement with the Folin phenol reagent","volume":"193","author":"LOWRY H., N.","year":"1951","unstructured":"LOWRY , 0. H., N. J. ROSEBROUGH , A. L. FARR , Am R . J. RANDALL. 1951 . Protein measurement with the Folin phenol reagent . J. Biol. Chem. 193 : 265 - 275 .","journal-title":"J. Biol. Chem."},{"key":"p_9","doi-asserted-by":"crossref","unstructured":"PETERSON E. A. AND H. A. SOBER. 1962. Column chromatography of proteins: substituted cellu- loses p. 3-32. In S. P. Colowick and N. 0. Kaplan [ed.] Methods in enzymology vol. 5. Academic Press Inc. New York.","DOI":"10.1016\/S0076-6879(62)05183-6"},{"key":"p_10","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1128\/JB.28.4.365-386.1934","article-title":"Cultivation of organisms concerned in the oxidation of thiosulfate","volume":"28","author":"STARKEY R. L.","year":"1934","unstructured":"STARKEY , R. L. 1934 . Cultivation of organisms concerned in the oxidation of thiosulfate . J. Bacteriol. 28 : 365 - 386 .","journal-title":"J. Bacteriol."},{"key":"p_11","first-page":"384","article-title":"Isolierungund krystallization der enolase","volume":"310","author":"WARBURG O.","year":"1942","unstructured":". WARBURG , O. , AN W. CHRIS rl AN. 1942 . Isolierungund krystallization der enolase . Biochem. Z. 310 : 384 - 421 .","journal-title":"Biochem. Z."}],"container-title":["Journal of Bacteriology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jb.95.1.87-94.1968","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jb.95.1.87-94.1968","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T17:26:57Z","timestamp":1627579617000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/jb.95.1.87-94.1968"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1968,1]]},"references-count":11,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1968,1]]}},"alternative-id":["10.1128\/jb.95.1.87-94.1968"],"URL":"https:\/\/doi.org\/10.1128\/jb.95.1.87-94.1968","relation":{},"ISSN":["0021-9193","1098-5530"],"issn-type":[{"value":"0021-9193","type":"print"},{"value":"1098-5530","type":"electronic"}],"subject":[],"published":{"date-parts":[[1968,1]]},"assertion":[{"value":"2021-02-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}