Analysis of the human sperm proteome.
As part of our effort to identify putative protein targets for the development of male contraceptives, we performed an in-depth proteomic analysis of human sperm by liquid chromatography and tandem mass spectrometry. Motile sperm were collected from a single fertile individual and fractionated into detergent-soluble and detergent-insoluble fractions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis separation of these fractions, followed by manual cutting of the gel, yielded 35 gel sections for each fraction to include proteins across the full range of electrophoretic mobility. Proteomic analysis of these gel sections identified more than 1,760 proteins with high confidence, with 1,350 proteins identified in the soluble fraction, 719 identified in the insoluble fraction, and 309 identified in both fractions. This characterization of the human sperm proteome provides a high-resolution, physiologically relevant index of the proteins that comprise human sperm.
Women's Health Research Institute, Wyeth Research, 500 Arcola Rd., N3169, Collegeville, PA 19426, USA. johnstd2@wyeth.com
Daniel S
DS
Johnston
Joe
J
Wooters
Gregory S
GS
Kopf
Yongchang
Y
Qiu
Kenneth P
KP
Roberts
D000595:Amino Acid Sequence; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D020543:Proteome / Q000032:analysis / Q000302:isolation & purification*; D013094:Spermatozoa / Q000737:chemistry* / Q000166:cytology
D020543:Proteome