Identification of a 42K phosphoprotein of platelets modulated by collagen

The α-subunit of pyruvate dehydrogenase

Thomas M. Chiang, Ellen S. Kang, Andrew Kang

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 Mr protein has already been identified as the light chain of myosin whereas the identity of the 42,000 Mr protein had not been established. By use of biochemical and immunological techniques, the identify of the 42,000 Mr component of prelabeled platelets found in the 100,000g 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 100,000g supernatant during the preparative procedure. Increased phosphorylation of the 42,000 Mr protein occurred after collagen stimulation and was accompanied by diminished pyruvate dehydrogenase activity.

Original languageEnglish (US)
Pages (from-to)15-23
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume252
Issue number1
DOIs
StatePublished - Jan 1 1987

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Phosphoproteins
Platelets
Pyruvic Acid
Oxidoreductases
Collagen
Blood Platelets
Proteins
Pyruvate Dehydrogenase Complex
Immunologic Techniques
Myosin Light Chains
Phosphorylation
Mitochondria
Labeling
Molecular Weight
Molecular weight

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Identification of a 42K phosphoprotein of platelets modulated by collagen : The α-subunit of pyruvate dehydrogenase. / Chiang, Thomas M.; Kang, Ellen S.; Kang, Andrew.

In: Archives of Biochemistry and Biophysics, Vol. 252, No. 1, 01.01.1987, p. 15-23.

Research output: Contribution to journalArticle

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