THE COMPLETE AMINO-ACID-SEQUENCE OF PITUITARY CYSTATIN FROM CHUM SALMON

Authors
KOIDE Y NOSO T
Citation
Y. Koide et T. Noso, THE COMPLETE AMINO-ACID-SEQUENCE OF PITUITARY CYSTATIN FROM CHUM SALMON, Bioscience, biotechnology, and biochemistry, 58(1), 1994, pp. 164-169
Citations number
40
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
Journal title
Bioscience, biotechnology, and biochemistry → ACNP
ISSN journal
09168451
Volume
58
Issue
1
Year of publication
1994
Pages
164 - 169
Database
ISI
SICI code
0916-8451(1994)58:1<164:TCAOPC>2.0.ZU;2-4
Abstract
Cystatin, a cysteine proteinase inhibitor, was isolated from chum salm on (Oncorhynchus keta) pituitary glands by ion-exchange chromatography on Mono-Q, gel filtration on Superdex 75, and reverse-phase HPLC on a n ODS following ethanol-ammonium acetate extraction. Salmon pituitary cystatin was equipotent to chicken egg-white cystatin in the papain in hibitory assay. The cystatin consists of 111 amino acid residues with two disulfide linkages formed between 66-75 and 89-109, and has 43% id entical sequences with chicken egg-white cystatin with consensus seque nces of reactive sites, Gly(4), Gln-X-Val-X-Gly (48-52), and Ile(Val)- Pro-Trp (96-98).