Characterization of a new variant of human red cell carbonic anhydrase I, CA if London (Glu-102→Lys)
dc.contributor.author | Tashian, Richard E. | en_US |
dc.contributor.author | Carter, Nicholas D. | en_US |
dc.contributor.author | Tanis, Robert J. | en_US |
dc.contributor.author | Ferrell, Robert E. | en_US |
dc.date.accessioned | 2006-09-11T14:18:47Z | |
dc.date.available | 2006-09-11T14:18:47Z | |
dc.date.issued | 1973-12 | en_US |
dc.identifier.citation | Carter, N. D.; Tanis, R. J.; Tashian, R. E.; Ferrell, R. E.; (1973). "Characterization of a new variant of human red cell carbonic anhydrase I, CA if London (Glu-102→Lys)." Biochemical Genetics 10(4): 399-408. <http://hdl.handle.net/2027.42/44118> | en_US |
dc.identifier.issn | 0006-2928 | en_US |
dc.identifier.issn | 1573-4927 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/44118 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4129482&dopt=citation | en_US |
dc.description.abstract | A new inherited variant of red cell carbonic anhydrase I (CA I), designated CA If London, was discovered during a survey of 1615 individuals from London, England. No electrophoretic variants of the other isozyme of carbonic anhydrase CA II, were observed in the same survey. Sequence analysis of a lysine-blocked tryptic peptide believed to contain the amino acid substitution in CA If showed that the glutamyl residue at position 102 had been substituted by a lysyl residue. This substitution results in a net increase of two positive charges in the mutant enzyme. Densitometric scanning of the electrophoretically separated forms in the variant hemolysate indicates that the levels of the normal and variant enzymes are approximately equal. | en_US |
dc.format.extent | 483536 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-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Media | en_US |
dc.subject.other | Medical Microbiology | en_US |
dc.subject.other | Human Genetics | en_US |
dc.subject.other | Zoology | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | Biomedicine | en_US |
dc.title | Characterization of a new variant of human red cell carbonic anhydrase I, CA if London (Glu-102→Lys) | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Human Genetics, University of Michigan Medical School, Ann Arbor, Michigan | en_US |
dc.contributor.affiliationum | Department of Human Genetics, University of Michigan Medical School, Ann Arbor, Michigan | en_US |
dc.contributor.affiliationum | Department of Human Genetics, University of Michigan Medical School, Ann Arbor, Michigan | en_US |
dc.contributor.affiliationother | Department of Biochemistry, London Hospital Medical College, London, England | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 4129482 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/44118/1/10528_2004_Article_BF00485993.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF00485993 | en_US |
dc.identifier.source | Biochemical Genetics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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