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Recombinant, structually unique Kazal-type proteinase inhibitor retains activity when C-terminally extended and glycosylated

SYSNO ASEP	0022123
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Ostatní články
Title	Recombinant, structually unique Kazal-type proteinase inhibitor retains activity when C-terminally extended and glycosylated
Title	Rekombinantní, strukturně ojedinělý proteázový inhibitor Kazalova typu zůstává aktivní po prodloužení karboxylového konce a glykozylaci
Author(s)	Kludkiewicz, B. (PL) Kodrík, Dalibor (ENTU-I) Grzelak, K. (PL) Nirmala, X. (IN) Sehnal, František (ENTU-I)
Source Title	Protein Expression and Purification. - : Elsevier - ISSN 1046-5928 Roč. 43, č. 2 (2005), s. 94-102
Number of pages	9 s.
Language	eng - English
Country	US - United States
Keywords	fusion proteins ; glycosylation ; Kazal domain
Subject RIV	CE - Biochemistry
R&D Projects	IBS5007316 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
CEZ	AV0Z50070508 - ENTU-I, BC-A (2005-2011)
Annotation	Kazal-type serine proteinase inhibitor GmSPI2 from insect silk was expressed in Pichia pastoris as rhSPI2 with C-terminal hexahistidine tag, rtSPI2 extended with GluAlaAla at the N-terminus, and rfSPI2 with this N-terminal extension and a C-terminal tail of 22 residues (myc epitope and hexahistidine). A portion of rfSPI2 was O-glycosylated. GmSPI2 was active slightly on trypsin and highly on subtilisin and proteinase K. Activity on the two latter enzymes was enhanced in rhSPI2 and rfSPI2 but rtSPI2 was clearly less active than GmSPI2.
Workplace	Institute of Entomology (until 2005)
Contact	Helena Musilová, musilova@entu.cas.cz, Tel.: 387 775 216
Year of Publishing	2006

Number of the records: 1