Strukturně unikátní inhibitor rekombinantní proteázy typu Kazal udrží aktivitu, když je na konci prodloužen a glykosylován

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F05%3A00008707" target="_blank" >RIV/60076658:12310/05:00008707 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Structurally unique recombinant Kazal-type proteinase inhibitor retains activity when terminally extended and glycosylated

Popis výsledku v původním jazyce

Recombinant derivatives of the Kazal-type serine proteinase inhibitor GmSP12 (36 amino acid residues), which is a component of insect silk, were prepared in the expression vector Pichia pastoris. The rhSP12 had a C-terminal hexahistidine tag attached tothe GmSP12 sequence, rtSP12 was extended with GluAlaAla at the N-terminus, and rfSP12 included this N-terminal extension and a C-terminal tail of 22 residues (myc epitope and hexahistidine). A portion of the secreted rfS12 was O-glycosylated with a trimannosyl or hexamannosyl. The native inhibitor was active slightly on trypsin and highly on subtilisin and protemase K. The extended C-terminus in rhSP12 and rfSP12 enhanced activity on the two latter enzymes and rendered rfSP12 active on clastase and pronase, but abolished the inhibition of trypsin. The glycosylation of rfSP12 reduced its inhibitory activity to a level comparable with the native inhibitor. The rtSP12 with tripeptide extension at the N-terminus and no C-terminal modificati

Název v anglickém jazyce

Structurally unique recombinant Kazal-type proteinase inhibitor retains activity when terminally extended and glycosylated

Popis výsledku anglicky

Recombinant derivatives of the Kazal-type serine proteinase inhibitor GmSP12 (36 amino acid residues), which is a component of insect silk, were prepared in the expression vector Pichia pastoris. The rhSP12 had a C-terminal hexahistidine tag attached tothe GmSP12 sequence, rtSP12 was extended with GluAlaAla at the N-terminus, and rfSP12 included this N-terminal extension and a C-terminal tail of 22 residues (myc epitope and hexahistidine). A portion of the secreted rfS12 was O-glycosylated with a trimannosyl or hexamannosyl. The native inhibitor was active slightly on trypsin and highly on subtilisin and protemase K. The extended C-terminus in rhSP12 and rfSP12 enhanced activity on the two latter enzymes and rendered rfSP12 active on clastase and pronase, but abolished the inhibition of trypsin. The glycosylation of rfSP12 reduced its inhibitory activity to a level comparable with the native inhibitor. The rtSP12 with tripeptide extension at the N-terminus and no C-terminal modificati

Druh

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

CEP obor

ED - Fyziologie

OECD FORD obor

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Projekt

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Návaznosti

V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název periodika

Protein expression and purification

ISSN

1046-5928

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

94-102

Kód UT WoS článku

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EID výsledku v databázi Scopus

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