Open AccessAmino‐Acid Sequence of the 20000‐Molecular‐Weight Light Chain of Chicken Gizzard‐Muscle Myosin
Author(s) -
MAITA Tetsuo,
CHEN JiannI,
MATSUDA Genji
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb06354.x
Subject(s) - gizzard , myosin , performic acid , amino acid , peptide sequence , immunoglobulin light chain , chemistry , urea , biochemistry , peptide , size exclusion chromatography , protein primary structure , sequence (biology) , biology , enzyme , antibody , genetics , gene , paleontology
The light chain fraction was separated from chicken gizzard muscle myosin. After S ‐carboxymethylation or performic acid oxidation, two light chain components (20000‐M, and 17000‐ M r chains) were isolated by chromatography on a column of DEAE‐cellulose in the presence of 4 M urea. Tryptic peptides of the S ‐carboxymethylated 20000‐ M r chain were isolated, and their sequences were determined. The alignment of these tryptic peptides in the chain was deduced from the amino acid compositions and from the partial sequences of peptic peptides of the oxidized protein. The established sequence consists of 171 amino acids and its calculated molecular weight is 19692. Comparing the sequence with those of L‐2 chains from chicken and rabbit skeletal muscle myosins, 81 and 78 amino acid substitutions were recognized, respectively, including insertions and/or deletions.