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Mol. Hum. Reprod. Advance Access originally published online on September 28, 2005
Molecular Human Reproduction 2005 11(9):677-681; doi:10.1093/molehr/gah217
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© The Author 2005. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oupjournals.org

Fine resolution of human sperm nucleoproteins by two-dimensional electrophoresis

Tsuyoshi Yoshii1, Naoaki Kuji1,4, Setsuko Komatsu2, Kazuhiro Iwahashi1, Yudai Tanaka1, Hiroyuki Yoshida1, Akira Wada3 and Yasunori Yoshimura1

1Department of Obstetrics and Gynecology, Keio University School of Medicine, Tokyo, 2Department of Molecular Genetics, National Institute of Agrobiological Sciences, Tsukuba, 3Department of Physics, Osaka Medical College, Takatsuki, Osaka, Japan

4 To whom correspondence should be addressed at: Department of Obstetrics and Gynecology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku, Tokyo 160-8582, Japan. E-mail: naoaki{at}sc.itc.keio.ac.jp

Human sperm nucleoproteins consist of protamines and histones. Changes in composition of these proteins are thought to correlate with spermatogenesis and may be involved in some instances of male infertility. We sought to separate sperm nucleoproteins including variants of protamine using an improved two-dimensional electrophoretic method, with the aim of comprehensively analysing all sperm nucleoprotein constituents. After extracting nuclear basic proteins from the sperm of normal volunteers, we analysed these proteins on a gel sheet by a radical free, highly reducing method based on Kaltschmidt and Whittmann’s two-dimensional electrophoresis. Basic proteins from sperm nuclei were separated clearly into 12 spots. By amino acid sequence analysis, these spots corresponded to protamine 1 (P1)- (five spots), protamine 2 (P2)-related proteins (six spots) and testis-specific histone H2B (one spot). The N-terminal amino acid sequences of the six P2-related proteins were compatible with those of HPI1, HPI2, HPS1, HPS2, HP2 and HP3, and quantitative comparison could be performed. In conclusion, human sperm nucleoproteins including all P2-related variants could be analysed quantitatively with high resolution on a single electrophoretic gel.

Key words: histone/human/nucleoprotein/protamine/spermatozoa


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