1988•PubMedRequires access
Purification, characterization and amino-acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice.
Uda K, Masahiro Ogawa, Takahiro Shibata, Atsuo Murata, Takahiro Mori, Norihiro Kikuchi, Nobuo Yoshida, Susumu Tsunasawa, Fumio Sakiyama
Open publisher page 17 citations
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.