Purification of Oxalyl CoA Synthetase Enzyme from Lathyrus sativus and Raising of Antibodies
01 Jul 1992-Journal of Plant Biochemistry and Biotechnology (Springer India)-Vol. 1, Iss: 2, pp 97-100
TL;DR: OCS-1 and OCS-2 did not share any common epltopes as no cross-reaction was seen and the monospecificity of the antiserum was checked by immunoblotting.
Abstract: Oxalyl CoA synthetase, a key enzyme in the biosynthesis of β-oxalyl CoA synthetase, a key enzyme in the biosynthesis of days old seedlings of Lathyrus sativus using affinity chromatography and electroelution. The enzyme existed in three forms. They were designated as OCS-1, OCS-2 and OCS-3 and their molecular weights were found to be 63.1, 39.9 and 17.7 kDa, respectively. The antibodies were raised against all the three enzymes. The monospecificity of the antiserum was checked by immunoblotting. OCS-1 and OCS-2 did not share any common epltopes as no cross-reaction was seen.
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TL;DR: Exploitable genetic variability for β-ODAP has been observed for development of low ODAP varieties, which along with improved agronomic and detoxification practices can help reduce the risk of lathyrism.
128 citations
Cites methods from "Purification of Oxalyl CoA Syntheta..."
...A two-step reaction for the ODAP synthesis is postulated which involves two terminal enzymes, namely Oxalyl CoA synthetase and ODAP synthase (Lambein et al. 2007; Malathi et al., 1967, 1970; Sehgal et al., 1992)....
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13 May 2008
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