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Biology of Reproduction, Vol 11, 601-610, Copyright © 1974 by Society for the Study of Reproduction
1 Division of Cell Biology, Department of Biological Chemistry and Genetics, The
University of Texas Medical Branch, Galveston, Texas 77550 Ultrastructural localization of several nonspecific and nucleoside phosphatase activities
during spermiogenesis was studied in Chinese hamster testes. Acid phosphatase activity
was found in dense bodies, multivesicular bodies, and Golgi apparatuses of both spermatogenic cells and Sertoli cells, while no alkaline phosphatase activity was observed in the
seminiferous tubule, although peritubular tissue was positive. During early stages of acrosome formation, acid phosphatase activity was demonstrated in the Golgi apparatus and
in acrosomal granules. This enzyme could not be detected in the granule when the acrosomal cap was formed. Thiamine pyrophosphatase, inosine diphosphatase, and acid phosphatase were detected in Golgi complex of the early spermatid, but none of these three enzymes
were detected following caudal migration of the apparatus. This phenomenon indicates a
change in the physiologic status of the Golgi apparatus during spermatid maturation. Thiamine pyrophosphatase, inosine diphosphatase, and adenosine triphosphatase activities
were localized on the cell surface and between intercellular spaces of spermatogenic cells
and Sertoli cells throughout the seminiferous tubular cycle. In the spermatid, however,
the three enzymes were not observed on the plasma membrane in exonemal canal. Furthermore, along the opposing plasma membrane of adjacent spermatogenic cells mere traces
or no enzyme activities were present. The phenomenon indicates a membrane specialization
and suggests a metabolic relationship between Sertoli cells and spermatogenic cells.
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