Generation of force by single-headed myosin.
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Actomyosin↗
Biomedical subjects
K E Franks
Publications and source records attributed to K E Franks.
Comparative electrophoretic study of Mallory body and intermediate filament protein.
To investigate the possibility that Mallory bodies (MBs) are composed of intermediate filaments (IFs), the electrophoretic patterns of MB proteins from human liver were compared with the IF protein extracted from chicken gizzard smooth muscle and extracts of mouse liver which contained MBs. The human MB had a protein component which had a similar mobility as that of the IF protein extracted from smooth muscle. A similar protein band was found in the extracts of mouse liver which contained MBs. No protein band corresponding to actin protein was found in human MB protein. The IF-like protein was also present in control mouse liver extract. The estimated molecular weight of the IF protein was 54,000. The evidence suggests that MBs are, in part, composed of IF protein. The IF protein is a normal constituent of liver and smooth muscle.
Animals↗
Mallory bodies compared with microfilament hyperplasia.
The binding characteristics of Mallory bodies (MBs) induced in livers of mice fed a long-term diet of griseofulvin were compared with the hyperplastic microfilaments induced by chronic phalloidin injections and with the MBs derived from livers of alcoholic patients at autopsy. Using the indirect immunofluorescence technique, smooth muscle antibody was shown to bind the hyperplastic microfilaments but not the human or mouse MBs. Peroxidase-antiperoxidase was shown to bind the human and mouse MBs but not the hyperplastic microfilaments. The evidence supports the idea that MBs are not composed of microfilaments (actin). The affinity of mouse and human MBs for peroxidase-antiperoxidase suggests that the MBs from these two species are chemically similar.
Actins↗