01448nas a2200193   4500008004100000022001400041245010500055210006900160260007300229300001200302490000700314520068200321653003201003653002501035653003401060100001801094700001401112856012801126       2012                        eng d  a0141-813000aSlow-tight binding inhibition of pepsin by an aspartic protease inhibitor from streptomyces sp MBR040 aSlowtight binding inhibition of pepsin by an aspartic protease i  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcJUL  a165-1740 v513 a<p>The present article reports a low molecular weight aspartic protease inhibitor from a Streptomyces sp. MBR04 exhibiting a two-step inhibition mechanism against pepsin. The kinetic interactions revealed a reversible, competitive, slow-tight binding inhibition with an IC50 and K-i values of 4.5 nM and 4 nM respectively. The conformational changes induced upon inhibitor binding to pepsin was monitored by far and near UV analysis, demonstrated that the inhibitor binds to the active site and causes inactivation. Chemical modification of the inhibitor with WRK and TNBS abolished the antiproteolytic activity of the inhibitor. (c) 2012 Elsevier B.V. All rights reserved.</p>10aAspartic protease inhibitor10aLow molecular weight10aSlow-tight binding inhibition1 aMenon, Vishnu1 aRao, Mala  uhttps://library.ncl.res.in/content/slow-tight-binding-inhibition-pepsin-aspartic-protease-inhibitor-streptomyces-sp-mbr04-0