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Title: Demonstration of the phosphorylated intermediates of the Ca2+-transport ATPase in a microsomal fraction and in a (Ca2+ + Mg2+)-ATPase purified from smooth muscle by means of calmodulin affinity chromatography
Authors: Wuytack, Frank ×
Raeymaekers, Luc
De Schutter, G
Casteels, Rik #
Issue Date: Mar-1983
Series Title: Biochimica et Biophysica Acta vol:693 issue:1 pages:45-52
Abstract: Ca2+ -dependent hydroxylamine-sensitive phosphorylated proteins can be demonstrated in a microsomal fraction of porcine antrum (stomach) smooth muscle and in a Ca2+ -transport ATPase ((Ca2+ + Mg2+)-ATPase) purified from this tissue by means of a calmodulin affinity technique. These phosphoproteins represent the phosphorylated intermediates of the (Ca2+ + Mg2+)-ATPases. In the (Ca2+ + Mg2+)-ATPase purified from smooth muscle the phosphorylated intermediate has an Mr of 130000 corresponding to the value found for erythrocyte (Ca2+ + Mg2+)-ATPase. In the smooth muscle microsomal fraction this 130 kDa phosphoprotein can also be seen, although its intensity is usually very low compared to a corresponding phosphorylation at Mr 100000. Including La3+ together with Ca2+ during phosphorylation of the microsomes increased selectively the steady state-level of the 130 kDa phosphoprotein over the value of the 100 kDa one. The 100 kDa Ca2+ -dependent phosphoprotein could either indicate the presence of a (Ca2+ + Mg2+)-ATPase of the same type of sarcoplasmic reticulum of skeletal muscle, or it could represent a proteolytic product of the 130 kDa phosphoprotein.
URI: 
ISSN: 0006-3002
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Physiology Section (-)
Laboratory of Cellular Transport Systems
× corresponding author
# (joint) last author

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