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Localization of the amino acid substitution site in a fast migrating variant of human serum albumin
Author(s) -
ladarola P.,
Minchiotti L.,
Galliano M.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80237-4
Subject(s) - substitution (logic) , amino acid substitution , albumin , chemistry , human serum albumin , serum albumin , biochemistry , amino acid , computer science , gene , mutation , programming language
Albumin Mi/Fg is an Italian genetic variant of human serum albumin arising from a Lys → Glu substitution which has been located in a CNBr fragment (CNBr VII) corresponding to the ‐COOH terminal portion of the molecule [(1984) J. Chromatogr. 298, 336‐344]. Tryptic peptides of CNBr VII from normal and Mi/Fg albumin have been purified by reverse‐phase high‐performance liquid chromatography (RP‐HPLC) and submitted to comparative structural studies. The amino acid sequence of the tryptic peptide of Mi/Fg variant that differs from the corresponding fragment of the normal serum albumin shows that the Lys → Glu substitution responsible for this variant is located at postion 573. This region of the albumin molecule is involved in the binding of long chain fatty acids.