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Purification, characterization and amino-acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice. 1988
K Uda, and
M Ogawa, and
T Shibata, and
A Murata, and
T Mori, and
N Kikuchi, and
N Yoshida, and
S Tsunasawa, and
F Sakiyama
Second Department of Surgery, Osaka University Medical School, Japan.
We purified two pancreatic secretory trypsin inhibitors (PSTI-I and PSTI-II) from rat pancreatic juice. PSTI-I consisted of 61 and PSTI-II of 56 amino-acid residues. Their amino-acid sequences were similar (40 out of 56 amino acid residues of PSTI-II being identical with those of PSTI-I), but PSTI-I and PSTI-II appeared to be translation products of different genes. There was no difference in inhibitory properties between PSTI-I and PSTI-II.
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