Abstract
A screening for the enzyme L-myo-inositol-1-phosphate synthase [EC 5.5.1.4] has been made first time in both vegetative and reproductive parts of the representative members of pteridophytes: Lycopodium, Selaginella, Equisetum, Polypodium, Dryopteris, and Gleichenia. The enzyme has been partially purified following low-speed centrifugation, streptomycin sulphate precipitation, ammonium sulphate fractionation, chromatography on DEAE-cellulose and gel-filtration through Sephadex G-200, and characterised from the reproductive pinnules of Gleichenia glauca Smith. The enzyme has a pH optimum at 7.5. The Km for glucose-6-P and NAD+ were 0.922 × 10−3 M and 0.9 × 10−4 M, respectively. A basal activity of the enzyme has been recorded in absence of exogenous NAD+. The enzyme activity was augmented with NH4Cl, but heavy metals like Hg2+, Cu2+ and Zn2+ inactivated it.
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Abbreviations
- BSA:
-
bovine serum albumin
- G-6-P:
-
D-glucose-6-phosphate
- I-1-P:
-
L-myo-inositol-1-phosphate
- I-1-P synthase:
-
L -myo-inositol-1-phosphate synthase
- NAD:
-
nicotinamide adenine dinucleotide
- TCA:
-
trichloroacetic acid
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Chettri, D.R., Choudhuri, M., Mukherjee, A.K. et al. L-myo-inositol-1-phosphate synthase: partial purification and characterisation from Gleichenia glauca . Biol Plant 49, 59–63 (2005). https://doi.org/10.1007/s10535-005-0063-0
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DOI: https://doi.org/10.1007/s10535-005-0063-0