PRIMARY STRUCTURE OF HUMAN PANCREATIC SECRETORY TRYPSIN-INHIBITOR - AMINO-ACID SEQUENCE OF REDUCED S-AMINOETHYLATED PROTEIN
PRIMARY STRUCTURE OF HUMAN PANCREATIC SECRETORY TRYPSIN-INHIBITOR - AMINO-ACID SEQUENCE OF REDUCED S-AMINOETHYLATED PROTEIN
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DOI：
10.1016/0003-9861(77)90103-5
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发表时间：
1977-01-01
影响因子：
3.9
通讯作者：
GREENE, LJ
中科院分区：
文献类型：
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作者：
BARTELT, DC;SHAPANKA, R;GREENE, LJ
采用选择性胰蛋白酶和胰糜蛋白酶在s -2-氨基乙基半胱氨酸抑制剂上的水解反应和传统的小肽序列测定方法（减法Edman降解和外肽酶水解）相结合的方法测定人胰腺分泌型胰蛋白酶抑制剂的氨基酸序列。根据降解过程中每个阶段产物的氨基和羧基末端残基的鉴定，对肽进行排序。序列测定是在组织和胰液中存在的色谱形式的混合物上进行的，这些色谱形式在氨基酸组成、氨基末端残基、分子量和比活性方面是相同的，但在天冬酰胺含量和对酶水解的敏感性方面有所不同。与猪、牛、羊胰腺的同源抑制剂进行了氨基酸序列比较。
The amino acid sequence of human pancreatic secretory trypsin inhibitor was determined by a combination of selective trypsin and chymotrypsin hydrolysis reactions on the S-2-aminoethylcysteinyl inhibitor and conventional methods (subtractive Edman degradation and exopeptidase hydrolysis) for sequence determination of small peptides. The peptides were ordered on the basis of the identification of the amino- and carboxy-terminal residues of the products at each stage of the degradation procedure. The sequence determination was carried out on a mixture of chromatographic forms present in both tissue and pancreatic juice which are identical in amino acid composition, amino-terminal residues, molecular weight and specific activity, but differ only in asparagine content and susceptibility to enzymatic hydrolysis. The amino acid sequence of the human inhibitor corresponding to chromatographic form A3 is compared with homologous inhibitors from porcine, bovine and ovine pancreas.