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Characterization of Proteins from Boar Prostate


Address reprint requests to Pavla Maňásková, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, 166 37 Prague 6, Czech Republic. E-mail:


Maňásková P, Ryšlavá H, Tichá M, Jonáková V. Characterization of proteins from boar prostate. AJRI 2002; 48:283–290 © Blackwell Munksgaard, 2002

PROBLEM: Most components of seminal plasma are secreted by accessory sexual glands: seminal vesicle, prostate gland and bulbourethral gland. The portion of proteins secreted by prostate gland differs in various species. Characterization of boar prostate proteins is the subject of this communication.

METHODS OF STUDY: Proteins of boar prostate gland were separated by affinity chromatography on heparin-polyacrylamide to non-heparin-binding (H) and heparin-binding (H+) fractions. The H and H+ fractions were subjected to reverse phase high performance liquid chromatography (RP HPLC) and their elution profiles were compared with those of the H and H+ fractions of boar seminal plasma. The isolated proteins were characterized by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), immunodetection, N-terminal amino acid sequencing and mass spectrometry (MALDI).

RESULTS: The following proteins of boar prostate secretion were identified: β-microseminoprotein, serotransferrin, serum albumin, myoglobin and PSP I and PSP II spermadhesins.

CONCLUSION: Presented results demonstrate composition of the main proteins of boar prostate secretion. β-Microseminoprotein was found to be a major protein of prostate secretion. PSP I and PSP II, major proteins of the H fraction of boar seminal plasma, were found in boar prostate secretion in lower amounts. The major proteins of the H+ fraction of boar seminal plasma (AQN, AWN) were not detected in prostate secretion.