Aggregated forms of bull seminal plasma proteins and their heparin-binding activity.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F04%3A23033208" target="_blank" >RIV/68378050:_____/04:23033208 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/04:00000371 RIV/00216208:11310/04:7032

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Aggregated forms of bull seminal plasma proteins and their heparin-binding activity.

Popis výsledku v původním jazyce

Heparin-binding activity of bull seminal plasma proteins was shown to be dependent on their aggregation state. Protein fraction interacting with immobilized heparin was characterized by large polydispersity in the region of relative molecular mass of 60000 ů 100 000 while that not retained on the affinity carrier was present as aggregates with relative molecular mass >100 000. Components of heparin-binding and non-heparin-binding fractions were separated by RP HPLC and analyzed by SDS electrophoresis and N-terminal sequencing. Size exclusion chromatography of whole seminal plasma and heparin-binding proteins in the presence of D-fructose (as a component of seminal plasma) showed that the region of relative molecular masses of protein associated formswas shifted to lower values. An increase of heparin-binding activity of bull proteins, as determined by ELBA, correlates with a decrease of their aggregation state. The modulation of the aggregation state of bull proteins by seminal plasm

Název v anglickém jazyce

Aggregated forms of bull seminal plasma proteins and their heparin-binding activity.

Popis výsledku anglicky

Heparin-binding activity of bull seminal plasma proteins was shown to be dependent on their aggregation state. Protein fraction interacting with immobilized heparin was characterized by large polydispersity in the region of relative molecular mass of 60000 ů 100 000 while that not retained on the affinity carrier was present as aggregates with relative molecular mass >100 000. Components of heparin-binding and non-heparin-binding fractions were separated by RP HPLC and analyzed by SDS electrophoresis and N-terminal sequencing. Size exclusion chromatography of whole seminal plasma and heparin-binding proteins in the presence of D-fructose (as a component of seminal plasma) showed that the region of relative molecular masses of protein associated formswas shifted to lower values. An increase of heparin-binding activity of bull proteins, as determined by ELBA, correlates with a decrease of their aggregation state. The modulation of the aggregation state of bull proteins by seminal plasm

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Collection of Czechoslovak Chemical Communications

ISSN

0010-0765

e-ISSN

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Svazek periodika

69

Číslo periodika v rámci svazku

N/A

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

15

Strana od-do

616-630

Kód UT WoS článku

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EID výsledku v databázi Scopus

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