| Literature DB >> 2564675 |
K Arai1, K Huss, J Madison, F W Putnam, F M Salzano, M H Franco, S E Santos, M J Freitas.
Abstract
Conventional horizontal starch-gel electrophoresis in four buffer systems and structural studies were performed on four albumin variants, and the findings were compared with similar previous data. Albumins Coari I and Porto Alegre I have a previously unreported amino acid substitution (glutamic acid replaced by lysine at position 358, denoted 358 Glu----Lys). The alteration in albumin Porto Alegre II (501 Glu----Lys) is the same as that found for three alloalbumins of Asiatic origin, designated Vancouver, Birmingham, and Adana. Albumin Oriximiná I has the same exchange as albumin Maku (541 Lys----Glu). Some of these findings can be explained only by the occurrence of independent mutations at the same site in the albumin gene. They also point to a third cluster of mutations in that gene, indicating hypermutability in some of its segments.Entities:
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Year: 1989 PMID: 2564675 PMCID: PMC286796 DOI: 10.1073/pnas.86.6.1821
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205