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2006 | 28 | 2 |

Tytuł artykułu

Partial purification and characterization of L-myo-inositol-1-phosphate synthase of pteridophytic origin

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Myo-Inositol is an important metabolite for normal growth and development of all living organisms. The cellular level of myo-inositol is con-rolled by the enzyme L-myo- inositol-1-phosphate synthase (MIPS) [EC 5.5.1.4]. Appreciable level of MIPS activity was detected from the common pteridophytes like Dicranopteris, Diplazium, Diplopterygium, Equisetum, Lycopodium, Polypodium, Pteridium, Selaginella etc. available in Darjeeling Himalayas. The enzyme was partially purified from the reproduc-ive pinnules of Diplopterygium glaucum (Thunb.) Nakai. The purification obtained was about 81 fold and the recovery was about 13.5 %. The final enzyme preparation specifically utilized D-Glucose-6-phosphte and NAD+ as its substrate and co-factor respectively. It shows pH optima between 7.0 and 7.5 while the temperature maximum was at 35 °C. The enzyme activity was slightly inhibited by Na+ and Cd2+ and highly inhibited by Li+ and Hg2+. The Krn values for D-glucose-6-phosphate and NAD+ was found to be as 0.83 mM and 0.44 mM respectively while the Vmax values were 1.42 mM and 1.8 mM for D-glucose-6-phosphate and NAD+ respectively. The present study indicates the universal occurrence of this enzyme in all plant groups.

Wydawca

-

Rocznik

Tom

28

Numer

2

Opis fizyczny

p.101-107,fig.,ref.

Twórcy

autor
  • Darjeeling Government College, Darjeeling-734 101, WB, India
autor

Bibliografia

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Bibliografia

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