Nishio H, Matsui H, Etoh S, Moia L J, Tokuda M, Itano T, Hatase O
Department of Physiology, Kagawa Medical School, Japan.
Biochem Biophys Res Commun. 1992 Jan 15;182(1):34-8. doi: 10.1016/s0006-291x(05)80108-1.
Two isoforms of calcineurin beta subunit(beta 1 and beta 2) were identified in rat testis by a monoclonal antibody Va1. Both beta 1 and beta 2 were recovered in calmodulin binding protein fraction and showed calcium shift on SDS-polyacrylamide gel electrophoresis which is the specific character for EF-hand calcium binding protein. beta 2 showed same apparent molecular weight on SDS-PAGE as that of brain calcineurin beta and was found in wide variety of tissues. beta 1 was shown to have six amino acid polypepeptide sequence and it showed higher molecular weight than brain beta and was specific for testis.
通过单克隆抗体Va1在大鼠睾丸中鉴定出钙调神经磷酸酶β亚基的两种同工型(β1和β2)。β1和β2均在钙调蛋白结合蛋白组分中回收,并在SDS-聚丙烯酰胺凝胶电泳上显示出钙迁移,这是EF-手型钙结合蛋白的特异性特征。β2在SDS-PAGE上显示出与脑钙调神经磷酸酶β相同的表观分子量,并且在多种组织中均有发现。β1显示具有六个氨基酸的多肽序列,其分子量比脑β亚基高,且是睾丸特异性的。