Zobrazeno 1 - 10
of 153
pro vyhledávání: '"V, Jonáková"'
Autor:
Y-J, Yi, S W, Zimmerman, G, Manandhar, J F, Odhiambo, C, Kennedy, V, Jonáková, P, Maňásková-Postlerová, M, Sutovsky, C-S, Park, P, Sutovsky
Publikováno v:
International journal of andrology. 35(2)
Protein ubiquitination is a stable, covalent post-translational modification that alters protein activity and/or targets proteins for proteolysis by the 26S proteasome. The E1-type ubiquitin-activating enzyme (UBA1) is responsible for ubiquitin activ
Publikováno v:
Folia biologica. 47(4)
The heparin-binding activity of bull seminal plasma proteins was inhibited by D-fructose, D-glucose, inulin and glycogen; D-galactose, dextran and mannan had no effect. While the ejaculated sperm-heparin interaction was not influenced by the presence
Autor:
L, Veselský, V, Jonáková, J, Dostál, V, Holán, Z, Voburka, J, Drahorád, P, Manásková, B, Zelezná
Publikováno v:
American journal of reproductive immunology (New York, N.Y. : 1989). 44(6)
Immunosuppressive fraction of boar seminal vesicle fluid (ISF) was tested to muffle primary and secondary antibody responses to xenotranfusions. Contemporaneously, heparin non-binding fraction of seminal plasma (H- fraction), presumed to be identical
Publikováno v:
Folia biologica. 46(4)
Boar seminal plasma was separated into five protein fractions (I-V) (100, 55, 45, 30, 5-15 kDa) by gel filtration chromatography on Sephadex G-75 SF at pH 7.4. RP HPLC of protein fractions I-V and N-terminal sequencing of their individual components
Publikováno v:
Molecular reproduction and development. 56
Boar seminal plasma was separated into five protein fractions (I-V) (100, 55, 45, 30, 5-15 kDa) by gel chromatography on Sephadex G-75 SF at pH 7.2. RP-HPLC of protein fractions I-V and N-terminal sequencing of their individual components revealed th
Publikováno v:
Folia biologica. 46(2)
Intrauterine deposition of the immunosuppressive fraction from boar seminal vesicle fluid (ISF) led to a suppression of antibody response to soluble and corpuscular antigens in mice. By means of an immunofluorescent method using specific monoclonal a
Publikováno v:
Folia biologica. 44(1)
Heparin-binding proteins BHB 2-BHB 5 were purified from boar seminal plasma by affinity chromatography on a heparin-polyacrylamide column and reversed phase HPLC. Three of the proteins, BHB 3-BHB 5, were found to be identical to spermadhesins AQN 1-A
Publikováno v:
Folia biologica. 45(5)
Boar seminal plasma proteins were separated by affinity chromatography on immobilized heparin into two portions: heparin-binding (H+) and non-heparin-binding (H-) proteins. Gel chromatography of the H+ portion yielded four main protein fractions of15
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