Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification
dc.contributor.author | Chegwidden, W. Richard | en_US |
dc.contributor.author | Tashian, Richard E. | en_US |
dc.contributor.author | Christiansen, Erik | en_US |
dc.contributor.author | Johansen, Jack T. | en_US |
dc.date.accessioned | 2006-09-11T14:25:00Z | |
dc.date.available | 2006-09-11T14:25:00Z | |
dc.date.issued | 1984-07 | en_US |
dc.identifier.citation | Tashian, Richard E.; Johansen, Jack T.; Christiansen, Erik; Chegwidden, W. Richard; (1984). "Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification." Bioscience Reports 4(7): 573-579. <http://hdl.handle.net/2027.42/44191> | en_US |
dc.identifier.issn | 0144-8463 | en_US |
dc.identifier.issn | 1573-4935 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/44191 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6433999&dopt=citation | en_US |
dc.description.abstract | Purified carbonic anhydrase isozymes I, II, and III (CA I, CA II, CA III) from various sources were treated with 2,3-butanedione and their bicarbonate dehydration reactions followed. The specific activities of human and bovine CA I and CA II and chicken CA III were not affected by the butanedione treatment, whereas the activities of human, gorilla, and bovine CA III were rapidly activated. These findings suggest that one, or both, of the two arginyl residues which appear to be unique to the active sites of the mammalian CA III isozymes are modified by butanedione. | en_US |
dc.format.extent | 400381 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; The Biochemical Society ; Springer Science+Business Media | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | Life Sciences | en_US |
dc.subject.other | Animal Biochemistry | en_US |
dc.subject.other | Plant Sciences | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.title | Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemistry, Carlsberg Laboratory, DK-2500, Copenhagen Valby, Denmark; Department of Human Genetics, University of Michigan Medical School, 1137 E. Catherine St., 48109, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationother | Department of Chemistry, Carlsberg Laboratory, DK-2500, Copenhagen Valby, Denmark; Carlsberg Biotechnology Ltd. A/S, DK-2200, Copenhagen N, Denmark | en_US |
dc.contributor.affiliationother | Clinical Chemistry Laboratory, Kommunehospitalet, DK-1399, Copenhagen K, Denmark | en_US |
dc.contributor.affiliationother | Department of Biological Sciences, Sheffield City Polytechnic, S1 1WB, Sheffield, UK | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 6433999 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/44191/1/10540_2005_Article_BF01121914.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF01121914 | en_US |
dc.identifier.source | Bioscience Reports | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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