Adarsh S. Shetty

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The kynureninase-type enzymes of three fungi and one bacterium were isolated and examined kinetically for their ability to catalyze the hydrolysis of L-kynurenine and L-3-hydroxykynurenine. The phycomycete Rhizopus stolonifer was found to contain a single, constitutive enzyme with Km for L-3-hydroxykynurenine and L-kynurenine of 6.67 times 10-minus 6 and(More)
Kynureninase-type (L-kynurenine hydrolase, EC 3.7.1.3) activity has been found to be present in the livers of fish, amphibia, reptiles, and birds. In addition to past information concerning this enzyme activity in mammalian liver, it is now clear that all the major classes of vertebrates carry a highly specialized kynureninase-type enzyme, which we have(More)
This article provides an insight on detailed current advances in molecular understandings of periodontal ligament cells and the influence of orthodontic force on them in the light of recent advances in molecular and genetic sciences. It sequentially unfolds the cellular events beginning from the mechanical force initiated events of cellular responses to(More)
Experiments were conducted on Nicotiana tabacum, L. to study the relation in the grana among chlorophylls, carotenoids, and proteins. The effect of iron chlorosis on protein and pigment synthesis was studied at different stages of chlorosis using glycine-U-C(14). Pigments were separated by thin layer chromatography.Chlorophyll a, chlorophyll b, carotenoid,(More)
(i) Saccharomyces cerevisiae grown in the presence of 1.0 mM l-tryptophan slowly excreted fluorescent material that was chromatographically identifiable as 3-hydroxyanthranilate but did not excrete detectable amounts of anthranilate nor rapidly deplete the medium of l-tryptophan. Under similar growth conditions, Neurospora crassa rapidly excretes(More)
1. delta-Aminolaevulate dehydratase (EC 4.2.1.24) was purified 80-fold from tobacco leaves and its properties were studied. 2. The enzyme had optimum pH7.4 in potassium phosphate buffer, K(m)6.25x10(-4)m at 37 degrees and pH7.4, optimum temperature 45 degrees and an activation energy of 11100 cal./mole. 3. The enzyme lost activity when prepared in the(More)
A comparative analysis of the kynureninase-type activity found in various organisms has demonstrated two forms of enzyme. One, inducible by tryptophan, has a relatively low Km for L-kynurenine, and is found in microorganisms such as Pseudomonas fluorescens and Neurospora crassa. The other, unaffected by tryptophan, has a low Km for L-3-hydroxykynurenine and(More)
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