Arif Lodhi Muhammad, Iqbal Choudhary M, Malik Abdul, Ahmad Saeed
Dr. Panjwani Center for Molecular Medicine and Drug Research, University of Karachi, Karachi-75270, Pakistan.
J Enzyme Inhib Med Chem. 2008 Jun;23(3):400-5. doi: 10.1080/14756360701584653.
The lignans (1-8) isolated from the roots of Vitex negundo Linn. were screened against the serine proteases alpha-chymotrypsin, thrombin and prolyl endopeptidase. Compounds 3 and 4 were found to be active only against alpha-chymotrypsin and were noncompetitive and competitive inhibitors of the enzyme, respectively. Ki values were found to be in the range 31.75-47.11 microM.
对从蔓荆子(Vitex negundo Linn.)根部分离得到的木脂素(1 - 8)进行了针对丝氨酸蛋白酶α-胰凝乳蛋白酶、凝血酶和脯氨酰内肽酶的筛选。发现化合物3和4仅对α-胰凝乳蛋白酶有活性,分别为该酶的非竞争性和竞争性抑制剂。Ki值在31.75 - 47.11微摩尔范围内。