Search results

Sort By:

Limit search:

Zinc-binding proteins from boar seminal plasma - isolation, biochemical characteristics and influence on spermatozoa stored at 4°C

100%

Mogielnicka-Brzozowska M., Wysocki P., Strzeżek J., Kordan W.

Acta Biochimica Polonica

2011

vol. 58

issue 2

171-177

Affinity chromatography on Chelating Sepharose Fast Flow Gel-Zn2+ was used for fractionation of boar seminal plasma proteins. Approximately 30% of total boar seminal plasma proteins showed affinity for zinc ions (ZnBP fraction). Native electrophoresis (PAGE) of ZnBP revealed six protein fractions which separated into 27 bands under denaturing conditions (SDS/PAGE). Two-dimensional electrophoresis (2D PAGE) showed 148 polypeptides with isoelectric points mostly in the basic and neutral pH range. The zinc-binding proteins comprise mainly 10-20 kDa polypeptides which are probably members of the spermadhesin family. ZnBP present in the incubation mixture of spermatozoa stored for 1 or 24 h at 4 °C allowed preservation of a higher percentage of cells exhibiting linear motility in comparison to a control sample stored in PBS. Presented results indicate that proteins binding Zn2+ ions have a shielding effect on the sperm plasma membrane and acrosome of spermatozoa, protecting these structures against consequences of cold shock.

High sequence homology between protein tyrosine acid phosphatase from boar seminal vesicles and human prostatic acid phosphatase

100%

Wysocki P., Płucienniczak G., Strzeżek J.

Acta Biochimica Polonica

2009

vol. 56

issue 3

481-486

Boar seminal vesicle protein tyrosine acid phosphatase (PTAP) and human prostatic acid phosphatase (PAP) show high affinity for protein phosphotyrosine residues. The physico-chemical and kinetic properties of the boar and human enzymes are different. The main objective of this study was to establish the nucleotide sequence of cDNA encoding boar PTAP and compare it with that of human PAP cDNA. Also, the amino-acid sequence of boar PTAP was compared with the sequence of human PAP. PTAP was isolated from boar seminal vesicle fluid and sequenced. cDNA to boar seminal vesicle RNA was synthesized, amplified by PCR, cloned in E. coli and sequenced. The obtained N-terminal amino-acid sequence of boar PTAP showed 92% identity with the N-terminal amino-acid sequence of human PAP. The determined sequence of a 354 bp nucleotide fragment (GenBank accession number: GQ184596) showed 90% identity with the corresponding sequence of human PAP. On the basis of this sequence a 118 amino acid fragment of boar PTAP was predicted. This fragment showed 89% identity with the corresponding fragment of human PAP and had a similar hydropathy profile. The compared sequences differ in terms of their isoelectric points and amino-acid composition. This may explain the differences in substrate specificity and inhibitor resistance of boar PTAP and human PAP.

Refine search results

2 Acta Biochimica Polonica

1 2011

1 2009

2 Strzeżek J.

2 Wysocki P.

1 Kordan W.

1 Mogielnicka-Brzozowska M.

1 Płucienniczak G.

Search results

Zinc-binding proteins from boar seminal plasma - isolation, biochemical characteristics and influence on spermatozoa stored at 4°C

High sequence homology between protein tyrosine acid phosphatase from boar seminal vesicles and human prostatic acid phosphatase