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J. Biol. Chem., Vol. 265, Issue 14, 8205-8211, May, 1990
D Feder and JM Bishop
The purification of pp60c-src has been hampered by the low levels of
protein it represents in most cells and its tendency to undergo proteolysis
during purification. The discovery that the platelet expresses unusually
high levels of pp60c-src has made large-scale purification from a normal
source feasible. We have developed a method for the purification of intact
pp60c-src to near homogeneity from human platelets and have determined the
enzymatic properties of this purified protein in vitro. Rapid, high yield
purification of pp60c-src from isolated platelet membranes was achieved in
a two-step protocol involving sequential chromatography on an
anti-pp60c-src immunoaffinity matrix and phenyl-Sepharose. This protocol
yielded 0.5 mg of pp60c-src from 30 units of platelets. Using enolase as an
exogenous substrate, the specific activity of the enzyme was 25 nmol
P.min-1.mg-1. The Km for MnATP2- for enolase phosphorylation (2.2 microM)
was higher than for the autophosphorylation of pp60c-src (0.6 microM).
Maximal enzyme activity required either Mn2+ or Mg2+, and both ATP and GTP
could be utilized as the phosphate donor. Evidence is shown which indicate
that the autophophorylation of pp60c-src in vitro occurs through an
intramolecular mechanism and that this reaction is reversible.
Purification and enzymatic characterization of pp60c-src from human platelets [published erratum appears in J Biol Chem 1990 Aug 15;265(23):14056]
Department of Microbiology and Immunology, University of California Medical Center, San Francisco 94143.
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