Myosin from human erythrocytes.

Journal Article

We have purified myosin from human erythrocytes using methods similar to that for other cytoplasmic myosins with a yield of about 500 micrograms/100 ml of packed cells. It consists of a 200-kDa heavy chain and light chains of 26- and 19.5 kDa and therefore differs from the isozyme in platelets which has light chains of 20- and 15 kDa. At low ionic strength, the myosin forms short bipolar filaments like those of platelet myosin. Eight of eight monoclonal antibodies to platelet myosin also bind to erythrocyte myosin. Like most myosins, it has a high ATPase activity in the presence of Ca2+ or EDTA, but is inhibited by Mg2+. Myosin light-chain kinase transfers 1 phosphate from ATP to the 20-kDa light chain, and this stimulates the actin-activated ATPase. Thus, myosin may play a role in shape changes in the erythrocytes.

Full Text

Duke Authors

Cited Authors

  • Wong, AJ; Kiehart, DP; Pollard, TD

Published Date

  • January 10, 1985

Published In

Volume / Issue

  • 260 / 1

Start / End Page

  • 46 - 49

PubMed ID

  • 3155518

International Standard Serial Number (ISSN)

  • 0021-9258

Language

  • eng

Conference Location

  • United States