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Photolabeling of the integral proteins of skeletal muscle sarcoplasmic reticulum: comparison of junctional and nonjunctional membrane fractions.

Abstract：

:Rabbit skeletal muscle sarcoplasmic reticulum (SR) was fractionated by isopycnic density gradient centrifugation into longitudinal tubules (LSR) and terminal cisternae (TC). Junctional face membranes (JFM) were obtained by Triton X-100 treatment of the TC fraction (Costello, B., Chadwick, C., Saito, A., Chu, A., Maurer, A. and Fleischer, S. (1986) J. Cell Biol. 103, 741-753). Photoactivatable phospholipid analogs were introduced into LSR, TC, and JFM fractions to specifically label integral membrane proteins. Remarkably different labeling patterns were observed. Proteins of the following Mr were labeled and identified in the junctional sarcoplasmic reticulum (JFM): 350,000, 325,000, 80,000, 49,000, 37,000, 32,000, 30,000, and 6000. Polypeptides of Mr 105,000 (Ca2+-dependent ATPase), 77,000, 55,000, 41,000, 22,000, and 9000 (proteolipid) were labeled and found to be selectively localized in the nonjunctional sarcoplasmic reticulum (LSR). Calsequestrin, a key protein responsible for Ca2+ storage within the SR lumen, was never labeled, whether 1 mM CaCl2 was present or absent, and is termed a nonintegral membrane protein.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Volpe P,Gutweniger HE,Montecucco C

doi

10.1016/0003-9861(87)90646-1

subject

Has Abstract

pub_date

1987-02-15 00:00:00

pages

138-45

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(87)90646-1

journal_volume

253

pub_type

杂志文章

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