{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T12:13:23Z","timestamp":1774786403018,"version":"3.50.1"},"reference-count":26,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[1986,2,1]],"date-time":"1986-02-01T00:00:00Z","timestamp":507600000000},"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":[[1986,2]]},"abstract":"<jats:p>Ribulose 1,5-bisphosphate carboxylase-oxygenase (RuBPC-O) activity was greatly enhanced when Rhodopseudomonas sphaeroides was grown in a mineral salts medium supplied with 1.5% CO2 in hydrogen. Analysis of cell extracts by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that cells growing on 1.5% CO2 in H2 specifically accumulated RuBPC-O polypeptides. Quantitative immunological determinations revealed that accumulation of form I and form II RuBPC-O closely correlates with the increase of specific activity. However, the two enzymes appeared to be derepressed at different levels. Upon transfer from heterotrophic to autotrophic (1.5% CO2) growth conditions, the intracellular form I RuBPC-O concentration was augmented 17-fold, whereas the form II RuBPC-O content increased only fourfold. As a result, the form I-form II ratio changed from 0.5 to about 2.0. Since this change in the RuBPC-O ratio occurred in the early stage of growth, it suggests that form I RuBPC-O is required for growth under drastic CO2 limitation. The difference in the extent of derepression of form I and form II RuBPC-O also indicates that the synthesis of each enzyme is regulated somewhat independently of the other.<\/jats:p>","DOI":"10.1128\/jb.165.2.620-624.1986","type":"journal-article","created":{"date-parts":[[2016,11,2]],"date-time":"2016-11-02T20:57:18Z","timestamp":1478120238000},"page":"620-624","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":83,"title":["Independent regulation of synthesis of form I and form II ribulose bisphosphate carboxylase-oxygenase in Rhodopseudomonas sphaeroides"],"prefix":"10.1128","volume":"165","author":[{"given":"Y","family":"Jouanneau","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F R","family":"Tabita","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"p_1","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1104\/pp.77.4.828","article-title":"Immunological determination of phosphoenolpyruvate carboxylase and the large and small subunits of ribulose 1,5- bisphosphate carboxylase in leaves of the C4 plant pearl millet","volume":"77","author":"Bassett C. 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