The epididymides of rat testis were fixed in glutaraldehyde and cut as frozen sections. The sections were incubated in lead nitrate solution containing as a substrate either ATP, AMP, creatinine phosphate, beta glycerophosphate, or phenyl phosphate. Then they were postfixed in osmium tetroxide, embedded, sectioned, and examined with the electron microscope. In the sperm tail, when ATP is used as a substrate the reaction product (lead phosphate) is observed both in the tail filament complex and on the surface membrane of the mitochondrial helix of the middle piece. In the tail filament complex, this product is seen near the nine paired peripheral and two central filaments, and in the matrix between the outer coarse fibers. But the product is not observed within these filaments and fibers. In longitudinal sections, no periodicity of the deposits in the complex is observed. When the other phosphate compounds are used as substrates the reaction products appear on the surface membrane of the mitochondrial helix, and are not found in the tail filament complex. No distinctly different localization of the reaction products is observed when substrates other than ATP are used. Possible relationships between the structure and the function of the sperm tail are discussed in the light of these findings.
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1 May 1965
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May 01 1965
LOCALIZATION OF ADENOSINE TRIPHOSPHATASE ACTIVITY IN THE RAT SPERM TAIL AS REVEALED BY ELECTRON MICROSCOPY
Toshio Nagano
Toshio Nagano
From the Department of Anatomy, School of Medicine, Chiba University, Chiba, Japan
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Toshio Nagano
From the Department of Anatomy, School of Medicine, Chiba University, Chiba, Japan
Received:
June 15 1964
Online ISSN: 1540-8140
Print ISSN: 0021-9525
Copyright © 1965 by The Rockefeller Institute Press
1965
J Cell Biol (1965) 25 (2): 101–112.
Article history
Received:
June 15 1964
Citation
Toshio Nagano; LOCALIZATION OF ADENOSINE TRIPHOSPHATASE ACTIVITY IN THE RAT SPERM TAIL AS REVEALED BY ELECTRON MICROSCOPY . J Cell Biol 1 May 1965; 25 (2): 101–112. doi: https://doi.org/10.1083/jcb.25.2.101
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