Kinetics study on a novel natural inhibitor of alpha-chymotrypsin.
The mechanism of inhibition of alpha-chymotrypsin by benzoylsalireposide (1), a phenolic glycoside isolated from Symplocos racemosa, was investigated. Lineweaver-Burk and Dixon plots and their secondary replots showed that 1 was a non-competitive inhibitor of this enzyme with the Ki value of 29.60 microM.
Ahmad
Viqar Uddin
VU
Dr. Panjwani Center for Molecular Medicine and Drug Research, HEJ Research Institute of Chemistry, International Centre for Chemical Sciences, University of Karachi, Karachi-75270, Pakistan. vuahmad@cyber.net.pk
Lodhi
Muhammad Arif
MA
Abbasi
Muhammad Athar
MA
Choudhary
Muhammad Iqbal
MI
D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D006027:Glycosides / Q000737:chemistry / Q000302:isolation & purification / Q000493:pharmacokinetics* / Q000494:pharmacology; D019684:Magnoliopsida / Q000737:chemistry*; D015394:Molecular Structure; D010936:Plant Extracts / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000493:pharmacokinetics* / Q000494:pharmacology
D006027:Glycosides; D010936:Plant Extracts; D015842:Serine Proteinase Inhibitors; C539398:benzoylsalireposide; D002918:Chymotrypsin; C117608:alpha-chymotrypsin