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Number of items: 7.

Journal Article

Balakrishnan, CV and Ravindranath, SD and Rao, N Appaji (1975) Studies on nucleotidases in plants Dimerization of the crystalline mung bean nucleotide pyrophosphatase by 5-adenosine monophosphate and the properties of the dimerized enzyme. In: Archives of Biochemistry and Biophysics, 168 (1). 163 -170.

Ravindranath, SD and Kumar, A Ashok and Kumar, R Prema and Vaidyanathan, CS and Rao, N Appaji (1974) Mechanism of aromatic hydroxylation *1, , *2, , *3: Properties of a model for pyridine nucleotide-dependent flavoprotein hydroxylases. In: Archives of Biochemistry and Biophysics, 165 (2). 478 -484.

Balakrishnan, CV and Ravindranath, SD and Rao, NA (1974) Studies on nucleotidases in plants - Reversible denaturation of the crystalline mung bean nucleotide pyrophosphatase and the effect of adenylates on the native and renatured enzyme. In: Archives of Biochemistry and Biophysics, 164 (1). pp. 156-164.

Balakrishnan, CV and Ravindranath, SD and Rao, N Appaji (1974) Studies on nucleotidases in plants : Reversible denaturation of the crystalline mung bean nucleotide pyrophosphatase and the effect of adenylates on the native and renatured enzyme. In: Archives of Biochemistry and Biophysics, 164 (1). pp. 156-164.

Kumar, Prema R and Ravindranath, SD and Vaidyanathan, CS and Rao, Appaji N (1972) Mechanism of hydroxylation of aromatic compounds: II. Evidence for the involvement of superoxide anions in enzymatic hydroxylations. In: Biochemical and Biophysical Research Communications, 49 (6). pp. 1422-1426.

Prema Kumar, R and Ravindranath, SD and Vaidyanathan, CS and Appaji Rao, N (1972) Mechanism of hydroxylation of aromatic compounds: Evidence for the involvement of superoxide anion in a model system. In: Biochemical and Biophysical Research Communications, 48 (5). pp. 1049-1054.

Ravindranath, SD and Rao, N Appaji (1969) Nucleotidases in plants *1, , *2: III. Effect of metabolites on the enzyme hydrolyzing flavine adenine dinucleotide (FAD) from Phaseolus radiatus. In: Archives of Biochemistry and Biophysics, 133 (1). pp. 54-59.

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