The schedule of spermatogenesis is determined from the times necessary for cells labeled with tritium thymidine during premeiotic DNA synthesis to pass through the successive spermatogenic stages. A transition from a typically somatic histone rich in lysine, to a histone rich in arginine is shown to occur during spermatid stages. A later shift to a protamine is observed in the maturing sperm. These changes are characterized by the use of in situ staining methods. The transition to an arginine-rich histone is accompanied by incorporation of tritium-labeled arginine, hence reflects synthesis of new protein. Comparison of the timing of arginine and thymidine incorporation, and independent measurements of DNA, show that in contrast to the case of premitotic chromosome duplication, the histone synthesis in the spermatid is unaccompanied by DNA synthesis. During the initial histone change, fine filaments are formed within the nucleus, which aggregate to form lamellae. This fine structure is lost during maturation of the sperm.
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1 June 1960
Content prior to 1962 was published under the journal name
The Journal of Biophysical and Biochemical Cytology
Article|
June 01 1960
Schedule of Spermatogenesis in the Pulmonate Snail Helix aspersa, with Special Reference to Histone Transition
David P. Bloch,
David P. Bloch
From the Department of Zoology, University of California, Los Angeles
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Howard Y. C. Hew
Howard Y. C. Hew
From the Department of Zoology, University of California, Los Angeles
Search for other works by this author on:
David P. Bloch
From the Department of Zoology, University of California, Los Angeles
Howard Y. C. Hew
From the Department of Zoology, University of California, Los Angeles
Received:
September 24 1959
Copyright, 1960, by The Rockefeller Institute
1960
J Biophys and Biochem Cytol (1960) 7 (3): 515–531.
Article history
Received:
September 24 1959
Citation
David P. Bloch, Howard Y. C. Hew; Schedule of Spermatogenesis in the Pulmonate Snail Helix aspersa, with Special Reference to Histone Transition . J Biophys and Biochem Cytol 1 June 1960; 7 (3): 515–531. doi: https://doi.org/10.1083/jcb.7.3.515
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