Amino acid substitution and chemical characterization of a Japanese variant of carbonic anhydrase I: CA I Hiroshima-1 (86 Asp → Gly)
dc.contributor.author | Hewett-Emmett, David | en_US |
dc.contributor.author | Yu, Ya-Shiou L. | en_US |
dc.contributor.author | Kageoka, Takeshi | en_US |
dc.contributor.author | Stroup, Sharon K. | en_US |
dc.contributor.author | Tashian, Richard E. | en_US |
dc.date.accessioned | 2006-09-11T14:20:37Z | |
dc.date.available | 2006-09-11T14:20:37Z | |
dc.date.issued | 1981-06 | en_US |
dc.identifier.citation | Kageoka, Takeshi; Hewett-Emmett, David; Stroup, Sharon K.; Yu, Ya-Shiou L.; Tashian, Richard E.; (1981). "Amino acid substitution and chemical characterization of a Japanese variant of carbonic anhydrase I: CA I Hiroshima-1 (86 Asp → Gly)." Biochemical Genetics 19 (5-6): 535-549. <http://hdl.handle.net/2027.42/44139> | en_US |
dc.identifier.issn | 0006-2928 | en_US |
dc.identifier.issn | 1573-4927 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/44139 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6794561&dopt=citation | en_US |
dc.description.abstract | An electrophoretic variant of red cell carbonic anhydrase I, designated CA I Hiroshima-1, has been observed in 12 apparently unrelated individuals during a survey of 13,019 individuals from the cities of Hiroshima and Nagasaki, Japan. Analyses of tryptic and chymotryptic peptide patterns of this CA I variant purified from 8 of the 12 individuals revealed the same altered peptides in each case. Examination of the amino acid sequence of an altered tryptic peptide purified from one of the variants showed that the aspartic acid residue at position 86 was replaced by a glycine residue. Thermostability studies demonstrated that all samples of CA I Hiroshima-1 were less stable than normal CA I. The specific esterase ( p -nitrophenyl acetate) activities of the normal and variant CA I isozymes were essentially the same. The difference spectra of the normal and variant enzymes were essentially the same. The isoelectric focusing patterns of CA I Hiroshima-1 showed a different pattern of minor bands to those produced by normal CA I. The relative amounts of the normal and variant enzymes purified from single heterozygous individuals were similar. | en_US |
dc.format.extent | 691288 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 | Biomedicine | en_US |
dc.subject.other | Human Genetics | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | Zoology | en_US |
dc.subject.other | Carbonic Anhydrase I | en_US |
dc.subject.other | Human Variant | en_US |
dc.subject.other | Thermostability | en_US |
dc.subject.other | Isoelectric Focusing | en_US |
dc.subject.other | Back Mutation | en_US |
dc.title | Amino acid substitution and chemical characterization of a Japanese variant of carbonic anhydrase I: CA I Hiroshima-1 (86 Asp → Gly) | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | 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, 48109, Ann Arbor, MI; Department of Internal Medicine, University of Tokyo Medical School, Tokyo, Japan | en_US |
dc.contributor.affiliationum | Department of Human Genetics, University of Michigan Medical School, 48109, Ann Arbor, MI | en_US |
dc.contributor.affiliationum | Department of Human Genetics, University of Michigan Medical School, 48109, Ann Arbor, MI | en_US |
dc.contributor.affiliationum | Department of Human Genetics, University of Michigan Medical School, 48109, Ann Arbor, MI | en_US |
dc.contributor.affiliationum | Department of Human Genetics, University of Michigan Medical School, 48109, Ann Arbor, MI | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 6794561 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/44139/1/10528_2004_Article_BF00484625.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF00484625 | en_US |
dc.identifier.source | Biochemical Genetics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.