THE AMINO-ACID-SEQUENCE OF HUMAN PANCREATIC RIBONUCLEASE
THE AMINO-ACID-SEQUENCE OF HUMAN PANCREATIC RIBONUCLEASE
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DOI：
10.1016/0003-2697(84)90306-3
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发表时间：
1984-01-01
影响因子：
2.9
通讯作者：
GLITZ, DG
中科院分区：
文献类型：
--
作者：
BEINTEMA, JJ;WIETZES, P;GLITZ, DG
人胰腺核糖核酸酶的一级结构是通过对天然蛋白质的自动测序以及通过蛋白水解酶、溴化氰和羟胺裂解得到的多肽的分析而确定的。人胰腺核糖核酸酶与牛胰腺核糖核酸酶在37个位置上存在差异。此外，人类的酶在C末端还有3个残基。大约一半的酶分子含有连接到序列ASN-Met-Thr(34-36)的碳水化合物。另外两个ASN-X-Ser/Thr序列不含碳水化合物。人胰腺核糖核酸酶含有许多带正电荷的残基，尤其是在N末端附近，而带负电荷的残基则更多地集中在C末端附近。
The primary structure of human pancreatic RNase was determined by automatic sequencing of the native protein and by analysis of peptides obtained by cleavage with proteolytic enzymes, cyanogen bromide and hydroxylamine. Human pancreatic RNase differs at 37 positions from bovine pancreatic RNase. In addition the human enzyme has 3 more residues at the C-terminus. About half of the enzyme molecules contain carbohydrate attached to the sequence Asn-Met-Thr (34-36). Two other Asn-X-Ser/Thr sequences are carbohydrate free. Human pancreatic RNase contains many positively charged residues, especially near the N-terminus, while negatively charged residues are more concentrated near the C-terminus.