Ordered arrays of Ca2+-ATPase on the cytoplasmic surface of isolated sarcoplasmic reticulum.

Abstract:

:Isolated sarcoplasmic reticulum (SR) vesicles with polymerized calcium pump protein were freeze-dried and rotary shadowed following uranyl acetate stabilization. This technique allows direct observation of a single side of the vesicle without requiring optical filtering. The heads of individual ATPase molecules, projecting above the cytoplasmic surface, are clearly resolved in the replicas. Ca ATPase molecules form extensive arrays in vanadate-treated, rabbit SR vesicles and in gently isolated, native SR vesicles from scallop. Gentle isolation results in limited areas of orderly structure in native SR isolated from vertebrate muscles. Special attention is given to the effect of various shadow thicknesses on the appearance of the heads. This information is essential to the interpretation of images in the accompanying paper (Franzini-Armstrong, C., and D.J. Ferguson, 1985, Biophys. J., 48:607-615).

journal_name

Biophys J

journal_title

Biophysical journal

authors

Ferguson DG,Franzini-Armstrong C,Castellani L,Hardwicke PM,Kenney LJ

doi

10.1016/S0006-3495(85)83815-7

subject

Has Abstract

pub_date

1985-10-01 00:00:00

pages

597-605

issue

4

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(85)83815-7

journal_volume

48

pub_type

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