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Identification of a 42K phosphoprotein of platelets modulated by collagen: The α-subunit of pyruvate dehydrogenase

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
252
Issue
1
Identifiers
DOI: 10.1016/0003-9861(87)90003-8
Keywords
  • Regulation Of Metabolism And Of Enzyme Action
Disciplines
  • Biology
  • Chemistry
  • Medicine

Abstract

Abstract Platelets exposed to collagen sufficient to stimulate the release reaction show an increase in labeling of two intracellular proteins with molecular weights of 20,000 and 42,000. The 20,000 M r protein has already been identified as the light chain of myosin whereas the identity of the 42,000 M r protein had not been established. By use of biochemical and immunological techniques, the identify of the 42,000 M r component of prelabeled platelets found in the 100,000 g supernatant of freeze-thawed or sonicated cells appears to be one of the subunits of pyruvate dehydrogenase complex which is translocated from the mitochondria to the 100,000 g supernatant during the preparative procedure. Increased phosphorylation of the 42,000 M r protein occurred after collagen stimulation and was accompanied by diminished pyruvate dehydrogenase activity.

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