title: The complete amino acid sequence of pituitary cystatin from chum salmon.
abstract: Cystatin, a cysteine proteinase inhibitor, was isolated from chum salmon (Oncorhynchus keta) pituitary glands by ion-exchange chromatography on Mono-Q, gel filtration on Superdex 75, and reverse-phase HPLC on an ODS following ethanol-ammonium acetate extraction. Salmon pituitary cystatin was equipotent to chicken egg-white cystatin in the papain inhibitory assay. The cystatin consists of 111 amino acid residues with two disulfide linkages formed between 66-75 and 89-109, and has 43% identical sequences with chicken egg-white cystatin with consensus sequences of reactive sites, Gly(4), Gln-X-Val-X-Gly (48-52), and Ile(Val)-Pro-Trp (96-98).
authors.affiliation: School of Fisheries Sciences, Kitasato University, Iwate, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Koide
authors.forename: T
authors.initials: T
authors.lastname: Noso
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D015891:Cystatins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D010206:Papain / Q000037:antagonists & inhibitors; D010902:Pituitary Gland / Q000737:chemistry*; D012474:Salmon; D017386:Sequence Homology, Amino Acid
chemical_list: D015891:Cystatins; D010206:Papain