Deswal, Renu ; Sopory, Sudhir K. (1998) Biochemical and immunochemical characterization of Brassica juncea glyoxalase I Phytochemistry, 49 (8). pp. 2245-2253. ISSN 0031-9422
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Official URL: http://www.sciencedirect.com/science/article/pii/S...
Related URL: http://dx.doi.org/10.1016/S0031-9422(98)00334-3
Abstract
A homogenous preparation of glyoxalase I (S-lactoylglutathione-lyase, EC 4.4.1.5) was obtained from Brassica juncea seedlings. The enzyme is a heterodimer with 27,000 and 29,000 Mr subunits and native Mr of 56,000. The circular dichroic spectra of the protein showed characteristics of a distinctly helical protein, and magnesium affected the secondary structure. It is a zinc metalloenzyme. Amino acid modification studies suggested the involvement of histidine residues in catalysis. Apo-glyoxalase I was reactivated by divalent cations Mn2+ (0.5 Mm)>Mg2+ (5 Mm)>Zn2+ (0.05 Mm) and Ca2+ (0.01 Mm). Monospecific, polyclonal anti-glyoxalase I antibodies were raised, which showed its presence in seeds, roots, hypocotyl, cotyledon and different flower parts. They showed varied degree of cross reactivity with the extracts from various plants, yeast, bacteria and animal system.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Brassica juncea L.; Brassicaceae; Glyoxalase I; CD Spectrum Apoenzyme; Amino Acid Modification; Antibodies; Cross Reactivity |
| ID Code: | 49923 |
| Deposited On: | 21 Jul 2011 09:27 |
| Last Modified: | 21 Jul 2011 09:27 |
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