Antiproteolytic activity of goose pancreas: purification, inhibitory properties and amino-acid sequence of a Kazal type trypsin inhibitor.
A trypsin inhibitor of Kazal type has been isolated from goose pancreas by affinity chromatography on immobilized anhydrotrypsin, anion exchange and reverse phase HPLC. It inhibits bovine beta-trypsin with the association constant (Ka) of 5.99 x 10(8) M-1. The complete amino-acid sequence was determined following CNBr treatment. The protein comprised a total of 69 amino-acid residues, corresponding to a molecular mass of 7.7 kDa. The P1-P'1 reactive site bond of the inhibitor was localized at position Lys25-Met26. The amino-acid sequence of GPTI shows extremely high homology to that of other inhibitors isolated from pancreas of birds.
Wilimowska-Pelc
A
A
Institute of Biochemistry, University of Wrocław, Poland.
Stachowiak
D
D
Gładysz
M
M
Olichwier
Z
Z
Polanowski
A
A
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005777:Geese; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010179:Pancreas / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D014359:Trypsin Inhibitor, Kazal Pancreatic