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1
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Heparin- and Zn^2+-binding proteins from boar seminal plasma

100%
Hołody D., Strzeżek J.
Acta Biochimica Polonica
|
1999
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vol. 46
|
issue 4
935-939
EN
Low molecular mass, heparin-binding proteins from seminal plasma play an important role in gametes interaction whereas plasmatic Zn^{2+}-binding proteins stabilize chromatin and plasmalemma structures and protect spermatozoa in the female reproductive tract. By means of affinity chromatography the heparin- and Zn^{2+}-binding proteins were isolated from boar seminal plasma and both preparations were analyzed by reverse HPLC. Most of the proteins bound to heparine and Zn^{2+}-ions were classified as spermadhesins. Three fractions binding exclusively Zn^{2+} were isolated. They differ in amino-acid composition, content of glucosamine and content of protein components revealed by SDS/PAGE.
2
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The influence of chosen physico-chemical factors on proteolytic activity of the hatching liquid of Coregonus albula and C. lavaretus

81%
Luberda Z., Strzeżek J., Łuczyński M.
Acta Biochimica Polonica
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1992
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vol. 39
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issue 1
59-64
3
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The influence of metal ions and some inhibitors on the activity of the proteinase isolated from the hatching liquid of Coregonus peled

81%
Luberda Z., Strzeżek J., Luczyński M.
Acta Biochimica Polonica
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1990
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vol. 37
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issue 1
197-200
4
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Zinc-binding proteins from boar seminal plasma - isolation, biochemical characteristics and influence on spermatozoa stored at 4°C

81%
Mogielnicka-Brzozowska M., Wysocki P., Strzeżek J., Kordan W.
Acta Biochimica Polonica
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2011
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vol. 58
|
issue 2
171-177
EN
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.
5
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High sequence homology between protein tyrosine acid phosphatase from boar seminal vesicles and human prostatic acid phosphatase

81%
Wysocki P., Płucienniczak G., Strzeżek J.
Acta Biochimica Polonica
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2009
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vol. 56
|
issue 3
481-486
EN
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.
6
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The antigenic character of zinc-binding proteins and their localization in boar reproductive tract - A preliminary study

81%
Mogielnicka-Brzozowska M., Fraser L., Strzeżek J., Kordan W.
Acta Biochimica Polonica
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2013
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vol. 60
|
issue 2
255-258
EN
In this study immunoelectrophoretic and double immunodiffusion analyses were used to investigate the antigenic character of zinc-binding proteins (ZnBPs), whereas the indirect immunofluorescence technique was used to identify their origin in boar reproductive tract. The mmunoelectrophoretic analysis of ZnBPs of the seminal plasma resulted in the appearance of three antigenic protein complexes, while specific immunoreactivity patterns of the anti-ZnBP serum were detected by double immunodiffusion analysis. Indirect immunofluorescence technique confirmed that ZnBPs were secreted by different reproductive tract tissues, suggesting their contributions to the seminal plasma.
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