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1

Different properties of four molecular forms of protein kinase CK2 from Saccharomyces cerevisiae

100%
Domanska K., Zielinski R., Kubinski K., Sajnaga E., Maslyk M., Bretner M., Szyszka R.
Acta Biochimica Polonica
|
2005
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tom 52
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nr 4
CK2 is a pleiotropic constitutively active serine/threonine protein kinase composed of two catalytic α- and two regulatory β-subunits, whose regulation is still not well understood. It seems to play an essential role in regulation of many cellular processes. Four active forms of CK2, composed of αα'ββ', α2ββ', α'2ββ', and a free α'-subunit were isolated from wild-type yeast and strains containing a single deletion of the catalytic subunit. Each species exhibits properties typical for CK2, but they differ in substrate specificity and sensitivity to inhibitors. This suggests that each CK2 isomer may regulate different process or may differ in the way of its regulation.
2

The influence of different forms of orosomucoid on immune reaction

100%
Lyutov A. G., Aleshkin V. A., Novicova L. I., Pukhalsky A. L.
Folia Histochemica et Cytobiologica
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1992
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tom 30
|
nr 4
3

Rola receptorow jadrowych w indukcji form molekularnych cytochromu P-450 pod wplywem substancji obcych

67%
Palut D., Kostka G., Strucinski P.
Roczniki Państwowego Zakładu Higieny
|
2002
|
tom 53
|
nr 4
321-332
Omówiono mechanizmy leżące u podstaw indukcji podrodziny CYP2B, ЗА i 4A oraz udział w tych procesach heterodimerycznych receptorów jądrowych.
4
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Molecular forms of selected antioxidant enzymes in dog semen – electrophoretical identification

67%
Koziorowska-Gilun M., Strzezek R.
Polish Journal of Veterinary Sciences
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2011
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tom 14
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nr 1
The aim of the study was the electrophoretical identification of molecular forms of selected antioxidant enzymes in dog semen. Ejaculates to be studied were chosen from five dogs, aged from two to eight years. Polyacrylamide gel electrophoresis was carried out under non-denaturing conditions and then gels were stained for the activity of the following enzymes: superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx). Sperm homogenates and all fractions (pre-spermatic, spermatic and post-spermatic) of dog ejaculate demonstrated one protein band with SOD activity characterized by low electrophoretic mobility. Based on the confirmed sensitivity to H₂O₂, it can be assumed that the detected SOD is an enzyme containing ions of Zn²⁺ and Cu²⁺ (Cu,Zn SOD). In sperm homogenates one protein band with GPx activity was characterized by high electrophoretic mobility, whereas in the spermatic and post-spermatic fractions of dog ejaculate three protein bands with different (low, medium and high) electrophoretic mobility were identified. CAT molecular forms were not found in either sperm homogenates or in the analyzed fractions of ejaculate.
5

Is the phosphorylation status of tyrosine proteins a marker for the cryo-capacitation of boar spermatozoa?

67%
Wysocki P., Koncicka K., Strzezek J.
Bulletin of the Veterinary Institute in Puławy
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2009
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tom 53
|
nr 2
229-232
The phosphorylation of tyrosine protein residues in spermatozoa was dependent on the semen of individual boars at different stages of the cryopreservation technology. Sperm proteins in the fresh semen of a boar with poor semen freezability (boar K) exhibited a higher content of phosphotyrosine residues compared to boars with better semen freezability (boars F and J). In the semen samples extended in a Kortowo 3 extender (K3) and cooled at 16°C, there was a marked increase in protein phosphorylation in the sperm proteins of boars with good semen freezability. This was manifested in the appearance of phosphoproteins with molecular weights of 17, 32, 43, 52, 63 and 78 kDa. In the case of boar K, the cooled-storage of K3-extended semen at 5°C caused the extensive phosphorylation of sperm proteins, with molecular weights of 45, 65 i 100 kDa. A gradual reduction in sperm protein tyrosine phosphorylation was detected in the extender containing lipoprotein fraction isolated from ostrich egg yolk (LPFo) compared with the K3 extender, what has no protective substances. It might be suggested that seminal plasma acid phosphatases, especially the vesicular molecular form of acid phosphatase (PTAP), played a very important role in the regulation of tyrosine phosphorylation in boar sperm plasmalemma proteins. Differences were observed in the number of dephosphorylated proteins by different molecular forms of phosphatases. It was shown that phosphotyrosine residues in sperm proteins could be completely dephosphorylated by the vesicular PTAP. It seemed that only sperm phosphotyrosine proteins, with molecular weights of 17, 32, and 63 kDa, could be dephosphorylated by the epididymal molecular form of acid phosphatase.
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