TY - JOUR
T1 - Ordered arrays of Ca2+-ATPase on the cytoplasmic surface of isolated sarcoplasmic reticulum
AU - Ferguson, D. G.
AU - Franzini-Armstrong, C.
AU - Castellani, L.
AU - Hardwicke, P. M.
AU - Kenney, L. J.
N1 - Funding Information:
We are grateful to Dr. John Weisel for the use of his optical diffractom- eter and Dr. John Murray for extensive advice and for calculating Fourier transforms from digitized images for us. The diffractometer was built with funds from the Biomedical Research Support Grant (Medical School and University of Pennsylvania), Nos. RR07083-17 and 2S07- RR-05415. We thank Mrs. D. Appelt-Byler for expert technical and photographic help, and Mr. D. Wray for microscope maintenance. This work was supported by grants from the National Institutes of Health (HL 15835-11) to the Pennsylvania Muscle Institute, and from National Science Foundation (PCM82-02516) and the Muscular Dystrophy Asso- ciation to Dr. C. Cohen. D. G. Ferguson is a fellow of the Alberta Heritage Foundation for Medical Research and L. Castellani is a fellow of the The Charles A. King Trust.
PY - 1985
Y1 - 1985
N2 - 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).
AB - 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).
UR - http://www.scopus.com/inward/record.url?scp=0022271367&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022271367&partnerID=8YFLogxK
U2 - 10.1016/S0006-3495(85)83815-7
DO - 10.1016/S0006-3495(85)83815-7
M3 - Article
C2 - 2932170
AN - SCOPUS:0022271367
SN - 0006-3495
VL - 48
SP - 597
EP - 605
JO - Biophysical journal
JF - Biophysical journal
IS - 4
ER -