摘要
利用Phenyl-Sepharose和Sephacryl S-200柱层析,从家兔阑尾B淋巴细胞中,部分纯化了一种新的钙结合蛋白(caBP)。用SDS-聚丙烯酰胺凝胶电泳(SDSPAGE)测得CaBP表观分子量为10400,而用凝胶过滤法测得分子量为21000,故称为CaBP_(21)。显然CaBP_(21)是由两个相同的亚基组成。CaBP_(21)等电点为5.4,在SDS-PAGE中的迁移不受Ca^(2+)的影响,而在非变性甘油PAGE中,有Ca^(2+)时迁移比缺Ca^(2+)时慢。CaBP_(21)对猪脑环核苷酸磷酸二酯酶(PDE)和鸡砂囊肌球蛋白轻链激酶(MLCK)活性均无影响。
By using Phenyl-Sepharose and Sephacryl S-200 chromatographies, a novel calcium-binding protein (CaBP) was isolated from rabbit appendix B lymphocytes and partially purified. The molecular weight of the purified CaBP was about 10400 as determined by SDS-PAGE and 21000 by gel filtration on Sephadex G-75.So we propose to designate it as CaBP21 that is composed of two identical subunits. The O isoelectric point (PI) of CaBP21 determined by electrofocusing was 5.4 ±0.1. The migration of CaBP21 on SDS-PAGE was the same in the presence and the absence of Ca2+, whereas on native-gel CaBP21 migrated more slowly in Ca2+ than in EGTA. CaBP21 show no stimulation ef f ecton brain cyclic nucleotide phosphodiesterase and chicken gizzard myosin light kinase.
关键词
阑尾
B细胞
钙结合蛋白
appendix
B lymphocyte
calcium-binding protein
