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001-es BibID:	BIBFORM079354
Első szerző:	Kandra Lili (biokémikus)
Cím:	Kinetic investigation of a new inhibitor for human salivary α-amylase / Kandra Lili, Zajácz Ágnes, Remenyik Judit, Gyémánt Gyöngyi
Dátum:	2005
ISSN:	0006-291X
Megjegyzések:	This study is the first report on the effectiveness and specificity of ?-acarviosinyl-(1 ? 4)-?-d-glucopyranosyl-(1 ? 6)-d-glucopyranosylidene-spiro-thiohydantoin (PTS-G-TH) inhibitor on the 2-chloro-4-nitrophenyl-4-O-?-d-galactopyranosyl-maltoside (GalG2CNP) and amylose hydrolysis catalysed by human salivary ?-amylase (HSA). Synthesis of PTS-G-TH was carried out by transglycosylation using acarbose as donor and glucopyranosylidene-spiro-thiohydantoin (G-TH) as acceptor. This new compound was found to be a much more efficient HSA inhibitor than G-TH. The inhibition is a mixed-noncompetitive type on both substrates and only one molecule of inhibitor binds to the enzyme. Kinetic constants calculated from secondary plots are in micromolar range. Values of KEI and KESI are very similar in the presence of GalG2CNP substrate; 0.19 and 0.24 ?M, respectively. Significant difference can be found for KEI and KESI using amylose as substrate; 8.45 and 0.5 ?M, respectively. These values indicate that inhibition is rather uncompetitive than competitive related to amylose hydrolysis.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Kinetic analysis Mixed-noncompetitive 2-Chloro-4-nitrophenyl-4-O-β-d-galactopyranosyl-maltoside a-Acarviosinyl- (1 - 4)-a-D-glucopyranosyl-(1 - 6)-D-glucopyranosylidene-spiro-thiohydantoin
Megjelenés:	Biochemical And Biophysical Research Communications. - 334 : 3 (2005), p. 824-828. -
További szerzők:	Zajácz Ágnes Gálné Remenyik Judit (1965-) (kémia tanár, okleveles vegyész) Gyémánt Gyöngyi (1960-) (vegyész)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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