Kinetic evidence for two nucleotide binding sites on the calcium ATPase of sarcoplasmic reticulum

Biochemistry ◽  
1991 ◽  
Vol 30 (6) ◽  
pp. 1456-1461 ◽  
Author(s):  
Richard J. Coll ◽  
Alexander J. Murphy
1986 ◽  
Vol 49 (1) ◽  
pp. 108-109 ◽  
Author(s):  
S. Verjovski-Almeida ◽  
P.C. Carvalho-Alves ◽  
C.G. Oliveira ◽  
S.T. Ferreira

1984 ◽  
Vol 39 (11-12) ◽  
pp. 1137-1140 ◽  
Author(s):  
Pankaj Medda ◽  
Wilhelm Hasselbach

Abstract The affinity of the sarcoplasmic reticulum transport ATPase for calcium and ATP is not affected by lipid depriviation while vanadate binding is completely abolished. Lipid substitution restores vanadate binding as well as the vanadate induced disappearance of the enzyme’s high affinity calcium and nucleotide binding sites. Nucleotide binding is simultaneously restored with the displacement of vanadate from the enzyme following the occupation of its low affinity calcium binding sites.


FEBS Letters ◽  
1989 ◽  
Vol 254 (1-2) ◽  
pp. 8-12 ◽  
Author(s):  
Pia Jakobs ◽  
Hubertus E. Sauer ◽  
J.Oliver McIntyre ◽  
Sidney Fleischer ◽  
Wolfgang E. Trommer

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