Scalable and Secure Dynamic Key Management and Channel Aware Routing in Mobile Adhoc Networks

A MANET (Mobile Ad-hoc Network) is an infrastructure-less self configuring wireless networks of routers. Key management is at the center of providing network security via cryptographic mechanisms with a high-availability feature. Dynamic key is the efficient assistance for network scalability. Routing protocol used here is a form of reactive routing called CA-AOMDV and compared with Table driven routing called DSDV. Channel aware routing protocol quality of the channel which can be measured in terms of suitable metrics. This paper leads to an emphasis on Black hole attack and to develop a dynamic key framework using RSA algorithm

Studies on glutamine synthetase: purification of the enzyme from mung bean (Phaseolus aureus) seedlings and modulation of the enzyme-antibody reaction by the substrates

Glutamine synthetase (L-glutamate : ammonia ligase, EC 6.3.1.2) from Phaseolus aureus (mung bean) seedlings was purified to homogeneity by ammonium sulphate fractionation, DEAE-cellulose chromatography, Sephadex G-200 gel filtration and affinity chromatography on histidine-Sepharose. The enzyme had a molecular weight of 775,000 ± 25,000. The enzyme consisted of identical subunits with an approximate subunit molecular weight of 50,000. Hyperbolic saturation curves were obtained with the substrates, glutamate, ATP and hydroxylamine. Antibody, raised in the rabbit, against mung bean glutamine synthetase, completely inhibited the activity of the enzyme. Preincubation of the enzyme with glutamate and ATP, prior to the addition of the antibody, partially protected the enzyme against inhibition. The Km values of this enzyme-antibody complex and the native enzyme were identical (glutamate, 2.5mM; ATP, 1 mM; hydroxylamine, 0.5 mM). The Km values of the partially inhibited enzyme (the enzyme pretreated with antibody prior to the addition of substrates) were 2-fold higher than those of the native enzyme. These results suggested that the substrate-induced conformational changes in the enzyme were responsible for the protection against inhibition of the enzyme activity by the antibody