ISSN:
0091-7419
Keywords:
Life Sciences
;
Molecular Cell Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Previous work has shown that the dynein from axonemes of sea urchin sperm consists of two distinct fractions which differ substantially in their extractability by salt. Upon gel electrophoresis of whole demembranated axonemes solubilized with sodium dodecyl sulfate, the dynein fraction shows two closely spaced bands with apparent molecular weights of 520,000 and 460,000; the proteins in these bands are termed the A and B components of the dynein. Similar electrophoresis of the soluble fraction obtained by extracting the axonemes with 0.5 M NaCl shows a single prominent band containing approximately half of the A component of the dynein (A1 component). The residue of extracted axonemes contain the other half of the A component of the dynein (A2 component) and all the B component. Densitometry of the bands indicates that the A1, A2 and B components of the dynein are present in approximately equal molar quantity. Electron microscopic studies show that the A1 component of the dynein constitutes the outer arms on the doublet tubules. Assay of ATPase activity in 0.05 M KCl and l mM ATP indicates about 65% of the total ATPase activity becomes soluble when the A1 component of the dynein is extracted with salt.
Additional Material:
3 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jss.400010603
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