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001-es BibID:	BIBFORM023504
Első szerző:	Gyémánt Gyöngyi (vegyész)
Cím:	Inhibition of human salivary [alpha]-amylase by glucopyranosylidene-spiro-thiohydantoin / Gyöngyi Gyémánt, Lili Kandra, Veronika Nagy, László Somsák
Dátum:	2003
Megjegyzések:	This study is the first report on the effectiveness and specificity of glucopyranosylidene-spiro-thiohydantoin (G-TH) inhibitor on the 2-chloro-4-nitrophenyl-4-O-beta-D-galactopyranosyl-maltoside (GalG2CNP) hydrolysis catalysed by human salivary alpha-amylase (HSA). The inhibition of hydrolysis is a mixed-noncompetitive type. In any case, only one molecule of inhibitor binds to HSA. Since our substrate and inhibitor are small molecules the long enough active site facilitates accommodating both of them simultaneously. However, the product formation can be excluded from enzyme-substrate-inhibitor complex (ESI) since Dixon plots are linear. Kinetic constants calculated from secondary plots and nonlinear regression are almost entirely equal, confirming the fidelity of the suggested model. Kinetic constants (Kli = 73mM, Lli = 2.84mM) show that G-TH is not such a potent inhibitor of HSA as acarbose and indicate higher stability for ESI than for enzyme-inhibitor complex.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban HSA Inhibitor Kinetic analysis Mixed-noncompetitive 2-Chloro-4-nitrophenyl-4-O-beta-D-galactopyranosyl-maltoside GalG2CNP Glucopyranosylidene-spiro-thiohydantoin G-TH
Megjelenés:	Biochemical and Biophysical Research Communications. - 312 : 2 (2003), p. 334-339. -
További szerzők:	Kandra Lili (1943-) (biokémikus) Nagy Veronika Somsák László (1954-) (vegyész)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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