Kamiya Y, Oyama F, Oyama R, Sakakibara F, Nitta K, Kawauchi H, Takayanagi Y, Titani K
Division of Biomedical Polymer Science, Fujita Health University, Aichi.
J Biochem. 1990 Jul;108(1):139-43. doi: 10.1093/oxfordjournals.jbchem.a123153.
The complete amino acid sequence and the location of disulfide bonds of a lectin from Japanese frog (Rana japonica) eggs, which specifically agglutinates transformed cells, are presented. The sequence was determined by analysis of peptides generated by digestion of the S-carboxyamidomethylated protein with Achromobacter protease I, or chymotrypsin, and by chemical cleavage with BNPS-skatole or cyanogen bromide. The lectin is a single-chain protein consisting of 111 residues, with a pyroglutamyl residue at the amino terminus. Four disulfide bonds link half-cystinyl residue 19 to 72, 34 to 82, 52 to 97, and 94 to 111. The sequence and the location of the disulfide bonds are highly homologous to those of bull frog (Rana catesbeiana) egg S-lectin. They are also homologous to human angiogenin, a tumor angiogenesis factor, and a family of pancreatic ribonucleases.
本文介绍了一种来自日本林蛙（Rana japonica）卵的凝集素的完整氨基酸序列及其二硫键位置，该凝集素能特异性凝集转化细胞。通过对经嗜无色杆菌蛋白酶I或胰凝乳蛋白酶消化的S-羧甲基化蛋白产生的肽段进行分析，以及用BNPS-粪臭素或溴化氰进行化学裂解来确定序列。该凝集素是一种由111个残基组成的单链蛋白，氨基端有一个焦谷氨酰残基。四个二硫键将半胱氨酰残基19与72、34与82、52与97以及94与111相连。其序列和二硫键位置与牛蛙（Rana catesbeiana）卵S-凝集素高度同源。它们也与人类血管生成素（一种肿瘤血管生成因子）以及一族胰腺核糖核酸酶同源。
