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.: Home > Animal Science Papers and Reports > 2007 > Volume 25 Number 4 > W³adys³aw Kordan1, Agata Malinowska2, Marek Lecewicz1, Pawe³ Wysocki1, Leyland Fraser1, Jerzy Strze؟ek1

The structure of platelet-activating factor acetylhydrolase (PAF-AH) isolated from boar seminal plasma and examined using mass spectrometry

W³adys³aw Kordan1, Agata Malinowska2, Marek Lecewicz1, Pawe³ Wysocki1, Leyland Fraser1, Jerzy Strze؟ek1
1 Department of Animal Biochemistry and Biotechnology, University of Warmia and Mazury in Olsztyn, Oczapowskiego 5, 10-718 Olsztyn-Kortowo, Poland, 2 Polish Academy of Sciences Institute of Biochemistry and Biophysics, Pawiٌskiego 5a, 02-106 Warsaw, Poland
Abstract :

Platelet-activating factor – acetylhydrolase (PAF-AH) – of boar seminal plasma is a heterogeneous
protein consisting of four polypeptides with molecular weights of 43, 55, 65 and 100 kDa. In 2004
the authors of the current report demonstrated that the N-terminal amino acid sequence of 43
kDa polypeptide is homologous with the amino acid sequences of the IgG-binding proteins and
zona pellucida-binding adhesion proteins. In the current report, due to the strongly blocked Nterminal amino groups of 55, 65 and 100 kDa polypeptides, their molecular structure was examined with mass spectrometry. In the PAF-AH complex structure the presence of epididymis-specific ل-mannosidase, fibronectin, spermadhesins AWN-1 and PSP-II, and IgG-binding proteins wasconfirmed. Determinations of the molecular weights of 55, 65 and 100 kDa enabled the identification of their peptide sequences and site of post-translational modifications.

Keywords :
acetylhydrolase / boar / mass spectrometry / platelet-activating factor / seminal plasma

Date Deposited : 08 Aug 2011 12:52

Last Modified : 08 Aug 2011 12:52

Official URL: http://www.ighz.edu.pl/

Volume 25, Number 4, - 2007

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