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Multiple forms of aspartate amino transferase from germinated green gram (Phaseolus aureus Roxb.).

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Title Multiple forms of aspartate amino transferase from germinated green gram (Phaseolus aureus Roxb.).
 
Creator Lalitha, K.
Patwardhan, M. V.
Radhakrishnamurthy, R.
 
Subject 07 Enzyme Biochemistry
22 Legumes-Pulses
 
Description L-Aspartate 2-oxoglutarate aminotransferases (EC 2.6.1.1), one from the supernatant and
three from the mitochondrial extract of 3-day old seedlings of green gram, have been purified and
some of their properties studied. The major supernatant enzyme (200-foid purified) moved as a
singie band of en~yme activity on polyacrylamide gel electrophoresis. All the partially purified
enzymes were anionic as shown by agar gel electrophoresis at pH 7·4. Kinetic studies indicated
a binary mechanism being operative. Data obtained on pH pattern, Km vaiues, eiectrophoretIc
and chromatographic studies· suggest isoenzymic nature of these enzyme forms.
 
Date 1974
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/4673/1/Indian%20Journal%20of%20Biochemistry%20%26%20Biophysics_11_1974_216-22-0.pdf
Lalitha, K. and Patwardhan, M. V. and Radhakrishnamurthy, R. (1974) Multiple forms of aspartate amino transferase from germinated green gram (Phaseolus aureus Roxb.). Indian Journal of Biochemistry and Biophysics, 11. pp. 216-220.