Labeling of high affinity ATP binding sites on the 53,000- and 160,000-dalton glycoproteins of the sarcoplasmic reticulum with the photoaffinity probe 8-N3-[alpha-32P]ATP.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Calcium Transport in Sarcoplasmic Reticulum
2. Molecular mechanism of active calcium transport by sarcoplasmic reticulum.
3. The sarcoplasmic calcium pump
4. Evidence for the participation of a Ca2+-dependent protein kinase and a protein phosphatase in the regulation of the Ca2+transport ATPase of the sarcoplasmic reticulum. 1. Effect of inhibitors of the Ca2+-dependent protein kinase and protein phosphatase
5. Evidence for the participation of a Ca2+dependent protein kinase and protein phosphatase in the regulation of the Ca2+transport ATPase of the sarcoplasmic reticulum. 2. Effect of phosphorylase kinase and phosphorylase phosphatase
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1. Identification of an Amino Acid in the ATP Binding Site of Na+/K+-ATPase after Photochemical Labeling with 8-Azido-ATP;Biochemistry;1994-04-12
2. Characterization and photoaffinity labeling of the ATP binding site of the ryanodine receptor from skeletal muscle;European Journal of Biochemistry;1993-04
3. Protein P4 of the bacteriophage phi 6 procapsid has a nucleoside triphosphate-binding site with associated nucleoside triphosphate phosphohydrolase activity;Journal of Virology;1992-10
4. Antibodies against the 53 kDa glycoprotein inhibit the rotational dynamics of both the 53 kDa glycoprotein and the Ca2+-ATPase in the sarcoplasmic reticulum membrane;Biochimica et Biophysica Acta (BBA) - Biomembranes;1991-04
5. Influence of the 53 kDa glycoprotein on the cooperativity of the Ca2+-ATPase of the sarcoplasmic reticulum;Biochimica et Biophysica Acta (BBA) - Biomembranes;1991-04
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