Journal of Plant Biochemistry and Biotechnology
  • Year: 1992
  • Volume: 1
  • Issue: 2

Purification of Oxalyl CoA Synthetase Enzyme from Lathyrus sativus and Raising of Antibodies*

  • Author:
  • Deepak Sehgal, I M Santha, S L Mehta
  • Total Page Count: 4
  • Page Number: 97 to 100

Division of Biochemistry, Indian Agricultural Research Institute, New Delhi-110 012, India

*Corresponding author.

*Part of the Ph.D. thesis submitted by senior author to the Post-Graduate School, IARI, New Delhi

Abstract

Oxalyl CoA synthetase, a key enzyme in the biosynthesis of p-oxalyl amino alanine (BOAA) was purified from three days old seedlings of Lathyrus salivus 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 an-tiserum was checked by immunoblotting. OCS-1 and OCS-2 did not share any common epitopes as no cross-reaction was seen.

Keywords

Lathyrus sativus, oxalyl CoA synthetase, antibodies