02543nas a2200205   4500008004100000022001400041245015800055210006900213260007900282300001400361490000700375520170700382653002202089653002002111653002402131653001802155100002102173700001402194856012902208       2009                        eng d  a0196-978100aDifferential elicitation of an aspartic protease inhibitor: regulation of endogenous protease and initial events in germination in seeds of vigna radiata0 aDifferential elicitation of an aspartic protease inhibitor regul  a360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USAbELSEVIER SCIENCE INCcDEC  a2118-21260 v303 a<p>Plant aspartic proteases are of recent origin with their physiological significance in crucial processes emerging. Reports on the significance of aspartic protease inhibitors and their endogenous proteases in seeds of plants are scanty. This paper reports the purification of an aspartic protease inhibitor from the seeds of Vigna radiata, its control of the endogenous aspartic protease and their subsequent role in the early germination events. The role of the aspartic protease inhibitor and the enzyme in initial stages of germination of V. radiata has been tracked by differential timed expression and germination assays. The expression pattern revealed maximum expression of the inhibitor in the dormant seeds while the enzyme was predominant in the germinating seeds. Their expression patterns and interactions indicate their significance in initiation of germination. The expression of other classes of proteases was monitored during germination and a model predicting the events occurring during proteolysis of the storage protein in germination is hypothesized. The inhibitor was a linear, hydrophobic, pH stable and thermostable peptide with molecular weight of 1660 Da. The purified inhibitor showed a pI of 4.36 with the sequence as AEIYN KDGNK LDLYG. The inhibitor was found to be stable in a broad range of pH from 2 to 10 with an optimum of 3.0. The half-life of VrAPI at 100 degrees C was 30 min whereas the maximum activity was observed at 37 degrees C. The initial kinetic analysis of the inhibitor against the enclogenous protease showed an IC50 value of 11 nM while the value of the inhibition rate constant K-i was 34 x 10(-9) M. (C) 2009 Elsevier Inc. All rights reserved.</p>10aAspartic protease10aPlant proteases10aProtease inhibitors10aVigna radiata1 aKulkarni, Aarohi1 aRao, Mala  uhttps://library.ncl.res.in/content/differential-elicitation-aspartic-protease-inhibitor-regulation-endogenous-protease-and-000523nas a2200157   4500008004100000022001400041245004400055210003900099260007500138300001200213490000700225100001400232700002300246700002100269856007500290       2016                        eng d  a0250-541X00aDr. V. Jagannathan (1921-2015) Obituary0 aDr V Jagannathan 19212015 Obituary  a5 LAJPATRAI RD, ALLAHABAD 211002, INDIAbNATL ACAD SCIENCES INDIAcAPR  a135-1360 v391 aRao, Mala1 aDeshpande, Vasanti1 aIngle, Prabhakar  uhttps://library.ncl.res.in/content/dr-v-jagannathan-1921-2015-obituary