{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T11:09:34Z","timestamp":1758280174369},"reference-count":50,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":8831,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1980,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Hamster fibroblast protein and rabbit hemoglobin were labelled by incubation of fibroblasts (BHK21) or reticulocytes with [<jats:sup>3<\/jats:sup>H]leucine. Alternatively, human or rabbit hemoglobin was labelled by carbamoylation of erythrocytes with K<jats:sup>14<\/jats:sup>CNO. The labelled hemoglobins were introduced into fibroblasts by virus\u2010mediated fusion between the blood cells and fibroblasts. The hemoglobins became uniformly distributed throughout the cytoplasm.<\/jats:p><jats:p>Degradation was assessed from release of acid\u2010soluble radioactivity into the medium. Radioactivity from [<jats:sup>14<\/jats:sup>C]\u2010carbamoylhemoglobin was released as carbamoylvaline and homocitrulline, and these compounds were not metabolized or reincorporated by the cells.<\/jats:p><jats:p>Intermediate degradation products could not be detected.<\/jats:p><jats:p>The degradation of hemoglobin followed first\u2010order kinetics. The half\u2010life of both carbamoylated and native rabbit hemoglobin in hamster fibroblasts was 28 h, and the half\u2010life of carbamoylated human hemoglobin was about 150 h in fibroblasts from hamster (BHK21), mouse (Balb\/3T3), and man (MRC 5), corresponding to that of the more stable endogenous proteins.<\/jats:p><jats:p>Phenylhydrazine increased the intracellular degradation of carbamoylated human hemoglobin about 13 times, whereas the degradation of endogenous proteins was little affected. Hemoglobin was degraded in homogenates at 31% h<jats:sup>\u22121<\/jats:sup> at pH 5 and 0.3% h<jats:sup>\u22121<\/jats:sup> at pH 7.4. Phenylhydrazine increased these rates to 45% h<jats:sup>\u22121<\/jats:sup> and 9.7% h<jats:sup>\u22121<\/jats:sup>, respectively.<\/jats:p><jats:p>Growing hamster fibroblasts, which are brought into quiescence by serum deprivation or by high culture density, increase the degradation of endogenous protein and of hemoglobin in parallel.<\/jats:p>","DOI":"10.1002\/jcp.1041050309","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T16:06:50Z","timestamp":1109434010000},"page":"449-460","source":"Crossref","is-referenced-by-count":27,"title":["Intracellular degradation of hemoglobin transferred into fibroblasts by fusion with red blood cells"],"prefix":"10.1002","volume":"105","author":[{"given":"Klavs B.","family":"Hendil","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.1040940110"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"3483","DOI":"10.1016\/S0021-9258(19)42598-2","article-title":"Regulation of protein synthesis during density\u2010dependent growth inhibition of BHK21\/13 cells","volume":"249","author":"Baenziger N. L.","year":"1974","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_4_1","first-page":"1","article-title":"Intracellular protein degradation","volume":"13","author":"Ballard F. J.","year":"1977","journal-title":"Essays Biochem."},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1400531"},{"key":"e_1_2_1_6_1","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1016\/S0021-9258(19)52400-0","article-title":"Incorporation in vitro of labeled amino acids into proteins of rabbit reticulocytes","volume":"196","author":"Borsook H.","year":"1952","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-5193(69)80012-3"},{"key":"e_1_2_1_8_1","volume-title":"Practical Haematology","author":"Dacie J. V.","year":"1970"},{"key":"e_1_2_1_9_1","volume-title":"Atlas of Protein Sequence and Structure","author":"Dayhoff M. O.","year":"1976"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1038\/257414a0"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-12-636150-6.50008-8"},{"key":"e_1_2_1_12_1","doi-asserted-by":"crossref","first-page":"3712","DOI":"10.1016\/S0021-9258(18)50643-8","article-title":"Identification and partial purification of an ATP\u2010stimulated alkaline protease from rat liver","volume":"254","author":"DeMartino G. N.","year":"1979","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1780305"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.130.3373.432"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.74.1.54"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(57)04059-8"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1730019"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0091-679X(08)60469-0"},{"key":"e_1_2_1_19_1","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/B978-0-12-636150-6.50017-9","volume-title":"Protein Turnover and Lysosome Function","author":"Goldberg A. L.","year":"1978"},{"key":"e_1_2_1_20_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.45.070176.003531"},{"key":"e_1_2_1_21_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(72)90136-1"},{"key":"e_1_2_1_22_1","doi-asserted-by":"publisher","DOI":"10.1016\/0968-0004(76)90001-3"},{"key":"e_1_2_1_23_1","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-12-636150-6.50016-7"},{"key":"e_1_2_1_24_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1740693"},{"key":"e_1_2_1_25_1","doi-asserted-by":"publisher","DOI":"10.1038\/258487a0"},{"key":"e_1_2_1_26_1","first-page":"345","volume-title":"Cellular and Molecular Biology of Erythrocytes","author":"Jaff\u00e9 E. R.","year":"1974"},{"key":"e_1_2_1_27_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1976.tb10175.x"},{"key":"e_1_2_1_28_1","doi-asserted-by":"crossref","first-page":"5861","DOI":"10.1016\/S0021-9258(19)43582-5","article-title":"Kinetics of the carbamylation of the amino groups of sickle cell hemoglobin by cyanate","volume":"248","author":"Lee C. K.","year":"1973","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_29_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.1040840304"},{"key":"e_1_2_1_30_1","doi-asserted-by":"publisher","DOI":"10.1139\/v55-050"},{"key":"e_1_2_1_31_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)52451-6"},{"key":"e_1_2_1_32_1","doi-asserted-by":"crossref","first-page":"6335","DOI":"10.1016\/S0021-9258(19)46935-4","article-title":"Is protein turnover thermodynamically controlled?","volume":"255","author":"McLendon G.","year":"1978","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_33_1","first-page":"485","article-title":"Cellular autophagocytosis induced by deprivation of serum and amino acids in HeLa cells","volume":"83","author":"Mitchener J. S.","year":"1976","journal-title":"Am. J. Pathol."},{"key":"e_1_2_1_34_1","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-12-636150-6.50009-X"},{"key":"e_1_2_1_35_1","doi-asserted-by":"crossref","first-page":"6221","DOI":"10.1016\/S0021-9258(19)43531-X","article-title":"Protein degradation in cultured cells","volume":"248","author":"Poole B.","year":"1973","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_36_1","first-page":"305","volume-title":"Membrane Fusion","author":"Poste G.","year":"1978"},{"key":"e_1_2_1_37_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0003-2697(69)80008-4"},{"key":"e_1_2_1_38_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0091-679X(08)60710-4"},{"key":"e_1_2_1_39_1","first-page":"93","volume-title":"Cellular and Molecular Biology of Erythrocytes","author":"Rapoport S. M.","year":"1974"},{"key":"e_1_2_1_40_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(79)90105-3"},{"key":"e_1_2_1_41_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(76)90499-X"},{"key":"e_1_2_1_42_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.75.3.807"},{"key":"e_1_2_1_43_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-88488-7"},{"key":"e_1_2_1_44_1","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.1016\/S0021-9258(18)91330-X","article-title":"On the reversible reaction of cyanate with sulfhydryl groups and the determination of NH2\u2010terminal cysteine and cystine in proteins","volume":"239","author":"Stark G. R.","year":"1964","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_45_1","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/S0021-9258(19)83983-2","article-title":"The use of cyanate for the determination of NH2\u2010terminal residues in proteins","volume":"238","author":"Stark G. R.","year":"1963","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_46_1","doi-asserted-by":"publisher","DOI":"10.1016\/0009-8981(61)90145-0"},{"key":"e_1_2_1_47_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-4827(79)90355-0"},{"key":"e_1_2_1_48_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(77)80639-X"},{"key":"e_1_2_1_49_1","doi-asserted-by":"publisher","DOI":"10.1002\/9780470719817.ch11"},{"key":"e_1_2_1_50_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(79)90213-7"},{"key":"e_1_2_1_51_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.1041000118"}],"container-title":["Journal of Cellular Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fjcp.1041050309","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/jcp.1041050309","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,12]],"date-time":"2023-11-12T16:03:30Z","timestamp":1699805010000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/jcp.1041050309"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1980,12]]},"references-count":50,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1980,12]]}},"alternative-id":["10.1002\/jcp.1041050309"],"URL":"https:\/\/doi.org\/10.1002\/jcp.1041050309","archive":["Portico"],"relation":{},"ISSN":["0021-9541","1097-4652"],"issn-type":[{"value":"0021-9541","type":"print"},{"value":"1097-4652","type":"electronic"}],"subject":[],"published":{"date-parts":[[1980,12]]}}}