%0 Journal Article
%T Purification and Trypsin Inhibitory Activity of Xenopus laevis Serum Albumin<br>非洲爪蟾血清白蛋白的分离纯化及胰蛋白酶抑制活性
%A ZHANG Ying-xia
%A LEE Wen-hui
%A ZHANG Yun
%A <br>张英霞
%A 李文辉
%A 张云
%J 动物学研究
%D 2005
%I Chinese Academy of Sciences
%X Frog albumin (XpA-serum) was purified from serum of Xenopus laevis by a combination of gel filtration and ion exchange chromatography steps. Like Bombina maxima albumin, XpA-serum exhibited trypsin inhibitory activity, which was lower than that of B. maxima albumin. XpA-serum at the concentration of 180 nM inhibited 84% activity of trypsin (30 nM). The equilibrium dissociation constants (KD) is 1.44×10-6 M as determined by Surface Plasmon Resonance. Western blot analysis revealed that XpA-serum was also distributed in the skin. It is deduced that serum albumin of amphibian possessing trypsin inhibitory activity can function directly or indirectly as a defensive substance against predators.
%K Amphibian
%K Xenopus laevis
%K Serum albumin
%K Trypsin inhibitor<br>两栖类
%K 非洲爪蟾
%K 血清白蛋白
%K 胰蛋白酶抑制剂
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=7C502F1A6798ACE1B8C57E291C48C7F1&aid=F1C2C9DC9FCB6006&yid=2DD7160C83D0ACED&vid=96C778EE049EE47D&iid=B31275AF3241DB2D&sid=6837BC93241057EF&eid=C824C8F9F54AE9B9&journal_id=0254-5853&journal_name=动物学研究&referenced_num=1&reference_num=9