Thromb Haemost 1974; 32(02/03): 678-684
DOI: 10.1055/s-0038-1647737
Original Article
Schattauer GmbH

Evidence for Ca2+ Regulated Magnesium ATPase of Thrombosthenin (Platelet Actomyosin)

C Mahendran*
1   Department of Biochemistry, Downstate Medical Center, State University of New York, Brooklyn, New York, U.S.A
› Author Affiliations
Further Information

Publication History

Received 04 March 1974

Accepted 06 August 1974

Publication Date:
30 June 2018 (online)

Summary

The isolation of an actomyosin-like protein from platelets with a Ca2+ sensitive component is described. The addition of 1 mM EGTA results in approximately 40% and 75% inhibition of the Mg-ATPase activity depending on the mode of isolation. The inhibition can be released by a free Ca2+ concentration of 3×l0-6 M. Superprecipitation is also inhibited by 1 mM EGTA and restored in the presence of 10-5 M free Ca2+.

* Present Address: Department of Neurology Mount Sinai School of Medicine of the City Univ. of New York Fifth Avenue and 100th street New York, New York 10029, U.S.A.


 
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