ISSN:
1573-4919
Keywords:
myosin subfragment-1
;
atrial myosin
;
myosin isoenzymes
;
ATPase activity
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Summary Subfragment-1 of rabbit atrial and thyrotoxic ventricular myosin (V1 isomyosin) has been prepared and purified by DEAF-cellulose column chromatography. Pyrophosphate-polyacrylamide gel electrophoretic patterns and column chromatographic profile of the atrial subfragment differ from those of thyrotoxic ventricular myosin subfragment-1. On the other hand, Ca2+, Mg2+ and actin-activated ATPase activities of these subfragments are identical. Comparison of the peptide mapping by limited proteolysis in the presence of sodium dodecyl sulfate of the heavy and the light subunits of these subfragments reveals that the patterns for the heavy chain peptides of these subfragments are substantially similar but their light chain peptide patterns differ. The results suggest that the enzymatic and structural similarities that have been recognized between these isoenzymes using intact myosin hold true for the myosin subfragment-1. The differences between these subfragments are due to the differences in the light chains associated with them.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00223198
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