Primary structure of sheep prostaglandin endoperoxide synthase deduced from cDNA sequence.

Abstract:

: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 Mr 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Yokoyama C,Takai T,Tanabe T

doi

10.1016/0014-5793(88)80847-0

subject

Has Abstract

pub_date

1988-04-25 00:00:00

pages

347-51

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(88)80847-0

journal_volume

231

pub_type

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