Beintema J J, Wietzes P, Weickmann J L, Glitz D G
Anal Biochem. 1984 Jan;136(1):48-64. doi: 10.1016/0003-2697(84)90306-3.
The primary structure of human (Homo sapiens) pancreatic ribonuclease has been determined by automatic sequencing of the native protein and by analysis of peptides obtained by cleavage with proteolytic enzymes, cyanogen bromide, and hydroxylamine. The following sequence was deduced: (sequence in text). Human pancreatic ribonuclease differs at 37 positions from bovine pancreatic ribonuclease. In addition the human enzyme has three 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 ribonuclease contains many positively charged residues, especially near the N-terminus, while negatively charged residues are more concentrated near the C-terminus.
人类（智人）胰腺核糖核酸酶的一级结构已通过对天然蛋白质的自动测序以及对用蛋白水解酶、溴化氰和羟胺裂解得到的肽段的分析得以确定。推导得到以下序列：（文本中的序列）。人类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，人类酶在C端还多三个残基。约一半的酶分子在Asn-Met-Thr（34 - 36）序列上连接有碳水化合物。另外两个Asn-X-Ser/Thr序列没有碳水化合物。人类胰腺核糖核酸酶含有许多带正电荷的残基，尤其是在N端附近，而带负电荷的残基则更集中在C端附近。
