title: A new type of low-molecular mass cysteine proteinase inhibitor from pig leukocytes.
abstract: A new low-molecular mass cysteine proteinase inhibitor (CPI) was purified from the cytosol of peripheral pig leukocytes. The isolation procedure included DEAE chromatography, Sephadex G-100 gel filtration and fast-protein liquid chromatography on Mono Q. The procedure resulted in the isolation of a homogeneous protein with a molecular mass of approximately 12 kDa and a pI of 4.8. The amino terminus is blocked. The amino-acid composition and the sequence of the C-terminal part of the molecule are suggestive of a new family of cystatins. The CPI was found to be a tight-binding inhibitor of both papain and cathepsin L, with Ki values of 0.1 nM and 1 nM, respectively.
authors.affiliation: Odsek za biokemijo, Institut J. Stefan, Univerza E. Kardelja, Ljubljana, Jugoslavija.
authors.forename: M
authors.initials: M
authors.lastname: Kopitar
authors.forename: A
authors.initials: A
authors.lastname: Ritonja
authors.forename: T
authors.initials: T
authors.lastname: Popovic
authors.forename: D
authors.initials: D
authors.lastname: Gabrijelcic
authors.forename: I
authors.initials: I
authors.lastname: Krizaj
authors.forename: V
authors.initials: V
authors.lastname: Turk
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002645:Chickens; D015853:Cysteine Proteinase Inhibitors / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007962:Leukocytes / Q000032:analysis*; D008722:Methods; D008969:Molecular Sequence Data; D013552:Swine
chemical_list: D000596:Amino Acids; D015853:Cysteine Proteinase Inhibitors