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Biology of Reproduction, Vol 22, 1007-1014, Copyright © 1980 by Society for the Study of Reproduction
1 Department of Zoology,
University of Iowa,
Iowa City, Iowa 52242 The protein constituents and iodinatable components of the spheroidal and ameboid forms of
Ascaris spermatozoa were characterized by SDS-gel electrophoresis, lactoperoxidase iodination and
[125I]-diazodiiodosulfanilic acid (DD125ISA) labeling. Electrophoresis of spermatozoan total
proteins on SDS-gels revealed 16 bands, two of which represent one major polypeptide (18,400
MW) and one major periodic acid-Schiff staining glycoprotein (12,000 MW). The spheroidal and ameboid spermatozoa shared four major components iodinatable by lactoperoxidase and DD125ISA methods. Three of these components have approximate molecular
weights of 51,000, 55,000 and 62,000, respectively. The molecular weight of the fourth component was extremely large as suggested by its position near the top of SDS-gel. In both forms
three small molecular weight components (10,000, 12,000 and 18,400 MW), minimally iodinated
by lactoperoxidase, were more extensively labeled with DD125ISA. The ameboid spermatozoa
differed from the spheroidal form in showing a decrease in iodination of the slowest electrophoretic band and in the presence of two iodinatable components (greater than 66,000 MW) not
detectable in the spheroidal form. These differences were evident in the iodination profiles of both
lactoperoxidase and DD125ISA methods. Both spheroidal and ameboid spermatozoa contain two molecular species of Conconavalin A
(Con A) receptors identified by histochemical staining after electrophoresis on SDS-gels. The
electrophoretic mobilities of these two Con A receptors are similar in the two forms of spermatozoa and are characterized by having large molecular weights; one receptor has a molecular
weight of 62,000, and the second has a molecular weight much greater than 66,000.
Accepted on February 12, 1980
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