{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,11,23]],"date-time":"2023-11-23T12:37:57Z","timestamp":1700743077041},"reference-count":28,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2008,6,28]],"date-time":"2008-06-28T00:00:00Z","timestamp":1214611200000},"content-version":"vor","delay-in-days":11532,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1976,12]]},"abstract":"<jats:p>Membrane\u2010bound <jats:sc>dd<\/jats:sc>\u2010carboxypeptidase of the unstable L\u2010form of <jats:italic>Proteus mirabilis<\/jats:italic> was solubilized by the non\u2010ionic detergent Genapol X\u2010100 and purified to protein homogeneity by affinity chromatography on ampicillin bound to succinyl\u2010aminododecyl\u2010cellulose. The purified enzyme with a molecular weight of 43000 is inhibited non\u2010competitively by penicillin G and carbenicillin, indicating a function of the penicillins as allosteric inhibitors. Sensitivity of the enzyme to penicillins is only moderate with a <jats:italic>K<\/jats:italic><jats:sub>i<\/jats:sub> of 1 \u03bcM for penicillin G. Breakdown of the enzyme\u2010inhibitor complex EI with different penicillins occurs rapidly with reappearance of active <jats:sc>dd<\/jats:sc>\u2010carboxypeptidase. The half\u2010life of EI with penicillin G is 5.5 min at 30 \u00b0C and 3.5 min at 37 \u00b0C, 10\u20131000\u2010fold shorter than EI half\u2010lives of <jats:sc>dd<\/jats:sc>\u2010carboxypeptidases in several other bacteria. The low stability of the enzyme\u2010inhibitor complex and the moderate penicillin sensitivity appear to be the basis for the continued activity of <jats:sc>dd<\/jats:sc>\u2010carboxypeptidase during growth of the L\u2010form and synthesis of peptidoglycan in the presence of high concentrations of penicillin.<\/jats:p>","DOI":"10.1111\/j.1432-1033.1976.tb11149.x","type":"journal-article","created":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T17:33:08Z","timestamp":1109871188000},"page":"585-593","source":"Crossref","is-referenced-by-count":16,"title":["Purification of the Membrane\u2010Bound <scp>dd<\/scp>\u2010Carboxypeptidase of the Unstable Spheroplast L\u2010Form of <i>Proteus mirabilis<\/i> by Affinity Chromatography"],"prefix":"10.1111","volume":"71","author":[{"given":"Hans Herbert","family":"MARTIN","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wolfgang","family":"SCHILF","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christian","family":"MASKOS","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,6,28]]},"reference":[{"key":"e_1_2_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/br.38.3.291-335.1974"},{"key":"e_1_2_3_3_2","doi-asserted-by":"publisher","DOI":"10.1099\/00221287-36-3-441"},{"key":"e_1_2_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(70)90268-8"},{"key":"e_1_2_3_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1975.tb02183.x"},{"key":"e_1_2_3_6_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac60030a007"},{"key":"e_1_2_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(67)11037-9"},{"key":"e_1_2_3_8_2","first-page":"220","volume":"10","author":"Maurer H. 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