Density and disposition of Ca2+-ATPase in sarcoplasmic reticulum membrane as determined by shadowing techniques.
We have studied the disposition of calcium ATPase in the native sarcoplasmic reticulum (SR) membrane of vertebrate muscles by rotary shadowing of freeze-dried isolated vesicles and of freeze-fractured in situ membranes. The predominant disposition of the ATPase molecules is disorderly, but small oligomers (dimers, tetramers, and occasionally larger aggregates) are seen. In vesicles from white hind legs of rabbits, the density of ATPase over nonjunctional SR is 31-34,000/microns2. ATPase density is always quite high, but small protein-free lipid patches may be interspersed with it.
Franzini-Armstrong
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C
Ferguson
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DG
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D005399:Fishes; D005612:Freeze Drying; D005614:Freeze Fracturing; D008854:Microscopy, Electron; D009132:Muscles / Q000201:enzymology / Q000648:ultrastructure; D011817:Rabbits; D011894:Rana pipiens; D012519:Sarcoplasmic Reticulum / Q000201:enzymology* / Q000648:ultrastructure
D000252:Calcium-Transporting ATPases