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Interaction between the Ca2(+)-ATPase and the proteolipid in artificial membranes.

作者信息

Jóna I, Martonosi A

机构信息

Department of Biochemistry, Suny, Upstate Medical Center, Syracuse 132101.

出版信息

Acta Physiol Hung. 1989;74(3-4):215-28.

PMID:2534829
Abstract

The interaction between the Ca2+ transport ATPase and the proteolipid of rabbit sarcoplasmic reticulum was analyzed by fluorescence energy transfer, using the following donor: acceptor combinations: Ca2(+)-ATPase tryptophan----IAEDANS-proteolipid; IAEDANS-ATPase----IAF-proteolipid; IAEDANS-proteolipid----IAF-ATPase. The observed energy transfer may indicate weak interaction between the Ca2(+)-ATPase and proteolipid, but collisional energy transfer definitely contributes. The energy transfer was abolished by deoxycholate or sodium dodecylsulfate at concentrations sufficient to solubilize the membrane. In view of the low proteolipid content of sarcoplasmic reticulum and the weak interaction suggested by the energy transfer, at best only a small fraction of ATPase molecules could exist in the form of ATPase-proteolipid complexes.

摘要

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