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淋巴细胞质膜一种新的68000道尔顿钙离子结合蛋白的分离与鉴定

Isolation and characterization of a novel 68,000-Mr Ca2+-binding protein of lymphocyte plasma membrane.

作者信息

Owens R J, Crumpton M J

出版信息

Biochem J. 1984 Apr 1;219(1):309-16. doi: 10.1042/bj2190309.

Abstract

A 68 000-Mr protein is a major component of a Nonidet P-40-insoluble fraction of lymphocyte plasma membrane prepared from human B lymphoblastoid cells ( BRI 8) and pig mesenteric lymph nodes. The association of the protein with the detergent-insoluble complex depends on free Ca2+ concentrations of greater than 10 microM. The human and pig 68 000-Mr proteins were purified and appear to be homologous on the basis of amino acid composition and peptide mapping. The protein is monomeric, has pI 5.8 and a single high-affinity Ca2+-binding site (KD 1.2 microM). The results are discussed in terms of the possible role of the 68 000-Mr protein as an intracellular Ca2+ receptor in lymphocytes.

摘要

一种68000道尔顿的蛋白质是从人B淋巴母细胞(BRI 8)和猪肠系膜淋巴结制备的淋巴细胞质膜的非离子去垢剂P - 40不溶性组分的主要成分。该蛋白质与去污剂不溶性复合物的结合取决于游离Ca2 +浓度大于10微摩尔。人源和猪源的68000道尔顿蛋白质被纯化,并且根据氨基酸组成和肽图谱分析显示它们似乎是同源的。该蛋白质是单体,其pI为5.8,有一个单一的高亲和力Ca2 +结合位点(解离常数KD为1.2微摩尔)。本文就68000道尔顿蛋白质作为淋巴细胞内Ca2 +受体的可能作用进行了讨论。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8079/1153478/74a668191fc4/biochemj00330-0304-a.jpg

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