Usami Y, Suzuki M, Yoshida E, Sakurai Y, Hirano K, Kawasaki T, Fujimura Y, Titani K
Department of Pharmaceutics, Gifu Pharmaceutical University, Japan.
Biochem Biophys Res Commun. 1996 Feb 27;219(3):727-33. doi: 10.1006/bbrc.1996.0302.
The complete amino acid sequences of alpha and beta subunits of alboaggregin-beta are presented. The alpha and beta subunits were separated by reversed-phase HPLC after reduction and S-pyridylethylation, and their sequences were determined by analysis of peptides generated by enzymatic or chemical digestion. The alpha and beta subunits consist of 133 and 123 amino acid residues, respectively. The sequences are highly homologous to each other (41.4% identity) and also to those of the alpha and beta subunits of botrocetin (a von Willebrand factor modulator) and the A and B chains of factor IX/X binding protein from other snake venoms. It is also homologous to C-type lectins with a homodimeric structure, but it shows no lectin-like activity.
本文给出了白聚凝血素-β的α和β亚基的完整氨基酸序列。α和β亚基在还原和S-吡啶基乙基化后通过反相高效液相色谱法分离，其序列通过对酶促或化学消化产生的肽段进行分析来确定。α和β亚基分别由133和123个氨基酸残基组成。这些序列彼此高度同源（同一性为41.4%），并且与博曲酶（一种血管性血友病因子调节剂）的α和β亚基以及来自其他蛇毒的因子IX/X结合蛋白的A链和B链的序列也高度同源。它也与具有同二聚体结构的C型凝集素同源，但不显示凝集素样活性。
