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Journal of Cell Science, Vol 15, 279-289, Copyright © 1974 by Company of Biologists

Submitted on April 11, 1973
Revised on January 21, 1974

Ultrastructural Evidence for Myosin of the Smooth Muscle Type at the Surface of Trypsin-Dissociated Embryonic Chick Cells

I. AP GWYNN 1, R. B. KEMP 1, B. M. JONES 1, and U. GRÖSCHEL-STEWART 2

1 Department of Zoology, University College of Wales, Aberystwyth, Wales, U.K.
2 Universitäts - Frauenklinik, Würzburg, West Germany

Cells dissociated from embryonic chick muscle tissue using trypsin were rotated in the presence of globulin-enriched rabbit antisera against both smooth and striated muscle actomyosins originating from chicken gizzard (GAM) and pectoralis (PAM) muscles respectively. The presence of the rabbit antibodies was demonstrated using peroxidase-labelled sheep anti-rabbit {lambda}-globulins, the enzyme-antibody conjugate being located by electron-microscope histochemistry.

Anti-GAM {lambda}-globulins reacted strongly with the plasma membrane. Judging from the complete absence of staining, {lambda}-globulins from non-immunized rabbit serum did not interact with the membrane.When {lambda}-globulins of sheep anti-rabbit IgG serum were applied alone, that is in the absence of pretreatment with rabbit {lambda}-globulin, there was an observable reaction with the cell surface. Preincubation of anti-GAM with the heavy meromyosin fraction from smooth-muscle myosin inhibited the interaction of the antibodies with the membrane, as evidenced by the absence of staining. A weak positive reaction obtained with anti-PAM was due to components of the antibody preparation which were reactive with actin and not with PAM.

It was concluded that a smooth-muscle myosin-like protein is an integral part of the plasma membrane of embryonic chick muscle cells.

Submitted on April 11, 1973
Revised on January 21, 1974






© The Company of Biologists Ltd 1974