Structural differences between the Ca2+-ATPase enzymes of sarcoplasmic reticulum membrane from rabbit and carp muscles.
1. Structural features were compared in sarcoplasmic reticulum Ca2+-ATPase enzymes from carp (Cyprinus carpio L.) and rabbit muscles. 2. Both membrane preparations contained the 105,000 mol. wt Ca2+ pump protein in high local density. 3. The tryptic cleavage of the carp enzyme gave different peptide fragments from those observed from rabbit enzyme. 4. Addition of vanadate, Ca2+ or lanthanides did not cause two-dimensional Ca2+-ATPase crystal formation, in contrast to the rabbit enzyme, which forms extensive arrays under these conditions. 5. No differences were found in this respect between microsome preparations derived from warm and cold adapted fishes. 6. A different primary sequence as well as a different disposition of the enzyme in the membrane may stand behind the observed dissimilarities.
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Department of Biochemistry, Albert Szent-Györgyi University Medical School, Szeged, Hungary.
Lelkes
G
G
Hieu
L H
LH
Nemcsók
J
J
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000302:isolation & purification*; D002347:Carps / Q000378:metabolism*; D003460:Crystallization; D003530:Cyprinidae / Q000378:metabolism*; D008854:Microscopy, Electron; D015394:Molecular Structure; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology / Q000648:ultrastructure; D010446:Peptide Fragments / Q000302:isolation & purification; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology / Q000648:ultrastructure; D013045:Species Specificity
D010446:Peptide Fragments; D000252:Calcium-Transporting ATPases