publication . Article . 2003

Isolation and characterization of euphorbain 1, a proteinase from the latex of Euphorbia lathyris

K.R. Lynn; N.A. Clevette-Radford;
  • Published: 11 Feb 2003 Journal: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, volume 746, pages 154-159 (issn: 0167-4838, Copyright policy)
  • Publisher: Elsevier BV
Abstract An enzyme showing some selectivity for bonds adjacent to leucine residues has been isolated as a homogeneous protein of molecular weight 43 000 from the latex of Euphorbia lathyris and is called euphorbain 1. Maximum protease activity was found at pH 7–7.5 and the pI is 4.9. The enzyme, unlike many previously studied proteases from plant sources, does not have a cysteinyl active centre, but is inhibited by diisopropyl fluorophosphate, suggesting that there is serine at the active site. The amino acid composition of euphorbain is reported, and is strikingly similar to that of cocoonase.
free text keywords: Biophysics, Biochemistry, Molecular Biology, Structural Biology
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