Purification, characterization and amino-acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice

K Uda; M Ogawa; T Shibata; A Murata; T Mori; N Kikuchi; N Yoshida; S Tsunasawa; F Sakiyama

Purification, characterization and amino-acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice

Biol Chem Hoppe Seyler. 1988 May:369 Suppl:55-61.

Authors

K Uda¹, M Ogawa, T Shibata, A Murata, T Mori, N Kikuchi, N Yoshida, S Tsunasawa, F Sakiyama

Affiliation

¹ Second Department of Surgery, Osaka University Medical School, Japan.

PMID: 3202973

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Hydrogen-Ion Concentration
Male
Molecular Sequence Data
Pancreatic Juice / analysis*
Protease Inhibitors
Rats
Rats, Inbred Strains
Trypsin Inhibitor, Kazal Pancreatic / analysis
Trypsin Inhibitor, Kazal Pancreatic / isolation & purification*
Trypsin Inhibitors / isolation & purification*

Substances

Protease Inhibitors
Trypsin Inhibitors
Trypsin Inhibitor, Kazal Pancreatic