Premium
Primary structure of sheep prostaglandin endoperoxide synthase deduced from cDNA sequence
Author(s) -
Yokoyama Chieko,
Takai Toshiyuki,
Tanabe Tadashi
Publication year - 1988
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(88)80847-0
Subject(s) - edman degradation , biochemistry , protein primary structure , peptide sequence , enzyme , proteolysis , peptide , carboxypeptidase , complementary dna , chemistry , serine , microbiology and biotechnology , amino acid , biology , gene
The complete amino acid sequence of prostaglandin endoperoxide synthase from sheep vesicular gland has been deduced by cloning and sequence analysis of DNA complementary to its messenger RNA. The results were confirmed by digestion of the enzyme with carboxypeptidase Y and by automated Edman degradation of the intact enzyme polypeptide and peptide fragments obtained by limited proteolysis of the enzyme with Achromobacter proteinase I. Mature sheep prostaglandin endoperoxide synthase is shown to be composed of 576 amino acids with an M r of 66 175. The precursor peptide is predicted to contain a 24‐residue signal peptide. The serine residue susceptible to acetylation by aspirin is found to be located near the C‐terminus of the enzyme polypeptide.