大鼠胰液中两种胰腺分泌型胰蛋白酶抑制剂的纯化、特性鉴定及氨基酸测序
Purification, characterization and amino-acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice.
作者信息
Uda K, Ogawa M, Shibata T, Murata A, Mori T, Kikuchi N, Yoshida N, Tsunasawa S, Sakiyama F
机构信息
Second Department of Surgery, Osaka University Medical School, Japan.
出版信息
Biol Chem Hoppe Seyler. 1988 May;369 Suppl:55-61.
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.
我们从大鼠胰液中纯化出两种胰腺分泌型胰蛋白酶抑制剂（PSTI-I和PSTI-II）。PSTI-I由61个氨基酸残基组成，PSTI-II由56个氨基酸残基组成。它们的氨基酸序列相似（PSTI-II的56个氨基酸残基中有40个与PSTI-I的相同），但PSTI-I和PSTI-II似乎是不同基因的翻译产物。PSTI-I和PSTI-II在抑制特性上没有差异。
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