Biochemical characterization of Acacia schweinfurthii serine proteinase inhibitor

Odei-Addo, Frank and Frost, Carminita and Smith, Nanette and Ogawa, Tomohisa and Muramoto, Koji and Gráf, László (2013) Biochemical characterization of Acacia schweinfurthii serine proteinase inhibitor. Journal of Enzyme Inhibition and Medicinal Chemistry (1-6). pp. 341-348. ISSN 1475-6366 (print), 1475-6374 (electronic) (Submitted)

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One of the many control mechanisms of serine proteinases is their specific inhibition by protein proteinase inhibitors. An extract of Acacia schweinfurthii was screened for potential serine proteinase inhibition. It was successfully purified to homogeneity by precipitating with 80% (v/v) acetone and sequential chromatographic steps, including ion-exchange, affinity purifica- Q2 tion and RP-HPLC. Reducing SDS-PAGE conditions revealed an inhibitor (ASTI) consisting of two polypeptide chains A and B of approximate molecular weights of 16 and 10 kDa, respectively, and under non-reducing conditions, 26 kDa was observed. The inhibitor was shown to inhibit bovine trypsin (Ki of 3.45 nM) at an approximate molar ratio of inhibitor: trypsin (1:1). The A- and B-chains revealed complete sequences of 140 and 40 amino acid residues, respectively. Sequence similarity (70%) was reported between ASTI A-chain and ACTI A-chain (Acacia confusa) using the ClustalW. The B-chain produced a 76% sequence similarity between ASTI and Leucaena leucocephala trypsin inhibitor.

Item Type: Article
Uncontrolled Keywords: Acacia schweinfurthii, amino acid sequence proteinase inhibitors, trypsin inhibitor
Subjects: Q Science / természettudomány > Q1 Science (General) / természettudomány általában
Depositing User: Dr. Balázs Jelinek
Date Deposited: 06 Feb 2014 16:15
Last Modified: 01 Feb 2015 00:15

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