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肌质网Ca2+-ATP酶的磷脂酶诱导晶体的二维结构。

Two-dimensional structure of phospholipase induced crystals of Ca2+-ATPase from sarcoplasmic reticulum.

作者信息

Misra M, Malhotra S K

出版信息

Biosci Rep. 1986 Dec;6(12):1065-70. doi: 10.1007/BF01141028.

DOI:10.1007/BF01141028
PMID:2953394
Abstract

A two-dimensional projection map was computed of the Ca2+-ATPase molecules in sarcoplasmic reticulum, isolated from rabbit skeletal muscle. Crystalline arrays of Ca2+-ATPase molecules were formed by incubating the membrane vesicles with phospholipase A2 and dialysing against Tris/HCl buffer. Ca2+-ATPase molecules appear as quasi-triangular blobs in the projection map and seem to form dimers. The projection map seems to indicate an enzyme conformation somewhat similar to vanadate-induced crystals but different from lanthanide-induced crystals of Ca2+-ATPase.

摘要

计算了从兔骨骼肌分离出的肌浆网中Ca2 + -ATP酶分子的二维投影图。通过用磷脂酶A2孵育膜囊泡并对Tris/HCl缓冲液进行透析,形成了Ca2 + -ATP酶分子的晶体阵列。在投影图中,Ca2 + -ATP酶分子呈现为准三角形斑点,似乎形成了二聚体。该投影图似乎表明一种酶构象,有点类似于钒酸盐诱导的晶体,但不同于镧系元素诱导的Ca2 + -ATP酶晶体。

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