Reiser G, Kunzelmann U, Hülser E, Stricker R, Hoppe J, Lottspeich F, Kalbacher H
Institut für Neurobiochemie der Otto-von-Guericke Universität Magdeburg, Germany.
Biochem Biophys Res Commun. 1995 Sep 5;214(1):20-7. doi: 10.1006/bbrc.1995.2251.
The aim of the present study was to identify a high affinity InsP4 receptor in membranes from cerebellum or brain from several species. In samples obtained from sheep, beef, human and rat, a 42 kDa protein represents an Ins(1,3,4,5)P4 receptor, similar to the InsP4 receptor from pig cerebellum, which we have described previously using an InsP4-photoaffinity analogue (Reiser et al., Biochem. J. 1991, 280, 533). CNBr cleavage of the pig receptor protein for peptide sequencing revealed peptide sequences which demonstrate that the 42 kDa InsP4 receptor is a novel protein. Two synthetic peptides derived from the pig receptor were used to generate peptide-specific antisera which recognized also the intact receptor protein from pig. The two antisera showed different reactivity with the InsP4 receptor purified from pig and human compared to sheep, beef, and rat. This indicates a species heterogeneity of this protein.
本研究的目的是在来自几个物种的小脑或大脑膜中鉴定一种高亲和力的肌醇四磷酸（InsP4）受体。在从绵羊、牛肉、人类和大鼠获得的样本中，一种42 kDa的蛋白质代表Ins(1,3,4,5)P4受体，类似于猪小脑的InsP4受体，我们之前使用InsP4光亲和类似物对此进行了描述（Reiser等人，《生物化学杂志》，1991年，280卷，533页）。对猪受体蛋白进行溴化氰裂解以进行肽测序，结果显示的肽序列表明该42 kDa的InsP4受体是一种新蛋白。源自猪受体的两种合成肽被用于产生肽特异性抗血清，这些抗血清也能识别来自猪的完整受体蛋白。与绵羊、牛肉和大鼠相比，这两种抗血清对从猪和人类纯化的InsP4受体表现出不同的反应性。这表明该蛋白存在物种异质性。
