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Molecular Cloning of the Human and Monkey Sperm Surface Protein PH-20
Ying Lin, Lida H. Kimmel, Diana G. Myles and Paul Primakoff
Proceedings of the National Academy of Sciences of the United States of America
Vol. 90, No. 21 (Nov. 1, 1993), pp. 10071-10075
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2363404
Page Count: 5
You can always find the topics here!Topics: Spermatozoa, Complementary DNA, Testes, Amino acids, RNA, Humans, Antigens, Cell membranes, Untranslated regions, Messenger RNA
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The guinea pig sperm surface protein PH-20 has an essential function in sperm adhesion to the zona pellucida of guinea pig eggs. Fully effective contraception has been achieved by immunizing either male or female guinea pigs with purified guinea pig PH-20. Here we report the isolation of human and cynomolgus monkey PH-20 cDNAs as a key step toward testing the function of primate PH-20 and the contraceptive efficacy of PH-20 immunization in primates. The deduced amino acid sequence of human PH-20 has 509 residues and is 59% identical with guinea pig PH-20, suggesting they may have a conserved function and immunogenicity. Southern blots show that there is a single PH-20 gene in the human genome and Northern blots of human testis poly(A)+ RNA show a 2.4-kb message. Northern blots of tissues other than testis are negative for PH-20, indicating that human PH-20 is testis-specific.
Proceedings of the National Academy of Sciences of the United States of America © 1993 National Academy of Sciences