Purification, characterization and amino-acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice.
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.
Uda
K
K
Second Department of Surgery, Osaka University Medical School, Japan.
Ogawa
M
M
Shibata
T
T
Murata
A
A
Mori
T
T
Kikuchi
N
N
Yoshida
N
N
Tsunasawa
S
S
Sakiyama
F
F
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008297:Male; D008969:Molecular Sequence Data; D010189:Pancreatic Juice / Q000032:analysis*; D011480:Protease Inhibitors; D051381:Rats; D011919:Rats, Inbred Strains; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000032:analysis / Q000302:isolation & purification*; D014361:Trypsin Inhibitors / Q000302:isolation & purification*
D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D014359:Trypsin Inhibitor, Kazal Pancreatic