title: Conversion of rat urinary prokallikrein to its active form.
abstract: A peptide derived from rat urinary prokallikrein by trypsin treatment comprised 7 amino acids, the sequence (Ala-Pro-Pro-Val-Gln-Ser-Arg) of which was identical with that of the N-terminal region in prokallikrein. Thus, with trypsin treatment, rat urinary prokallikrein is converted to the active form with the release of the N-terminal propeptide consisting of 7 amino acids. An Arg-1-Val+1 bond in the prokallikrein was found to be the site of proteolytic cleavage of the propeptide.
authors.affiliation: Department of Pharmacology, Osaka University of Pharmaceutical Sciences, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Takenobu
authors.forename: M
authors.initials: M
authors.lastname: Takaoka
authors.forename: E
authors.initials: E
authors.lastname: Suyama
authors.forename: M
authors.initials: M
authors.lastname: Yano
authors.forename: S
authors.initials: S
authors.lastname: Morimoto
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004792:Enzyme Precursors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007610:Kallikreins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D051381:Rats; D014357:Trypsin / Q000378:metabolism
chemical_list: D004792:Enzyme Precursors; D007610:Kallikreins; C052910:prokallikrein, tissue; D014357:Trypsin