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Biologia Plantarum

, Volume 49, Issue 1, pp 59–63 | Cite as

L-myo-inositol-1-phosphate synthase: partial purification and characterisation from Gleichenia glauca

  • D. R. Chettri
  • M. Choudhuri
  • A. K. Mukherjee
  • J. Adhikari
Article

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.

Additional key words

inositol synthase myo-inositol pteridophytes 

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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Copyright information

© Institute of Experimental Botany 2005

Authors and Affiliations

  • D. R. Chettri
    • 1
  • M. Choudhuri
    • 1
  • A. K. Mukherjee
    • 2
  • J. Adhikari
    • 3
  1. 1.Botany DepartmentDarjeeling Govt. CollegeDarjeelingIndia
  2. 2.Botany DepartmentBurdwan UniversityBurdwanIndia
  3. 3.Botany DepartmentPresidency CollegeCalcuttaIndia

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