Canine pancreatic kallikrein: enzyme isolation and characterization.
Two forms of canine pancreatic kallikrein, designated as canine pancreatic kallikrein A and B, were separately isolated by ion-exchange, affinity and hydrophobic chromatographies. These enzymes had similar apparent molecular masses, substrate specificities and pH optima. However, kallikrein B was inhibited by soybean trypsin inhibitor, while kallikrein A was not. Both kallikrein A and B were shown by sodium dodecyl sulfate-polyacryl amide gel electrophoresis to consist of two polypeptide chains, designated alpha and beta chains, and binding by disulfide bond(s). The N-terminal amino acid sequences of each alpha and beta chains of kallikrein A and B were determined.
Ohnishi
N
N
1st Department of Surgery, Faculty of Medicine, University of Tokyo, Japan.
Ikekita
M
M
Atomi
Y
Y
Kizuki
K
K
Moriya
H
H
Kondo
K
K
Yamada
H
H
Tsugita
A
A
D000595:Amino Acid Sequence; D000818:Animals; D004285:Dogs; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes; D007610:Kallikreins / Q000737:chemistry* / Q000187:drug effects / Q000302:isolation & purification / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism; D010179:Pancreas / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity; D014664:Vasodilation / Q000187:drug effects
D007527:Isoenzymes; D009842:Oligopeptides; D011480:Protease Inhibitors; D007610:Kallikreins