ISSN:
1432-0878
Keywords:
Actin
;
Myosin
;
Plasma membrane
;
Binding
;
Antibodies 125I
;
Autoradiography
;
Electron microscopy
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Summary 125I-labelled sheep anti-rabbit γ-globulin antibodies were used to locate rabbit antibodies to smooth- and striated-muscle actomyosins at the surface of trypsin-dissociated embryonic chick cells. Statistical analysis of electron microscope autoradiographs revealed that the plasma membrane of these cells was significantly labelled with both antibodies. Further tests revealed that there were a significantly greater number of antigenic sites present on the cell surface for the gizzard smooth-muscle antibodies than for those against pectoralis striated-muscle actomyosin. It was further shown that both the rate and extent of binding of the 125Ilabelled smooth-muscle actomyosin antibodies to the cells were greater than for anti-striated-muscle γ-globulins. Binding of the former was reduced to a level similar to that of 125I-NIS conjugate by preincubation of the y-globulins with smooth-muscle heavy meromyosin, while a similar reduction was observed when anti-pectoralis actomyosin was treated with actin. It was concluded that actin- and myosin-like proteins must now be considered as integral components of the plasma membrane. The authors wish to thank Dr. W. Sinclair (Zoology) and Miss S. Lutkins (Statistics Department) for assistance with the statistical analysis and are grateful to Professor N. A. Mitchison (Zoology Department, University College London) for providing a control sample of 125I-labelled sheep anti-rabbit γ-globulin, Dr. D. Catty (Experimental Pathology Department, Birmingham University) for donating sheep anti-rabbit serum and Dr. U. Gröschel-Stewart (Zoologisches Institut der TH., Darmstadt, Federal Republic of Germany) for the rabbit anti-actomyosin antibodies. Miss B. Morris and Messrs. P. C. Lloyd, D. Williams and J. Meredith gave skilled technical assistance
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00224659
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