ABSTRACT

Introduction: Literature review has revealed that the distribution of the enzymes of 6-phospo-gluconate dehydrogenase activities of some acetone derived tissues in animal tissue have so far not been investigated systematically. This leaves a gap for further investigation to explore the subject matter deeply.

Method: Barium salts of D-Glucose 6-phosphate (0 6-P), 6-phosphogluconate (6-PO) and D-ribose 5-phosphate (R 5-P) are available and were used in our study. (TNP) triphosphopyridine was prepared and analyzed; its composition was 75% TNP without (DNP) diphosphopyridine nucleotide.

      Ice-cold isotone KCL (0-15M-KCL with 8ml, 0-02M-KHCO3) was disintegrated in 09 parts. It is done in a potter glass homogenizer or in a Nelco homogenizer. This is followed by centrifuging and dialysis of the supernatants. Heparinized blood 10ml was used for erythrocyte hemolysis, which was diluted with 10ml of water. 01 part of haemolysate was treated with 9 parts of isotonic KCI.

      Spectroscope is used to determine the dehydrogenase activity of dialyzed tissue. The method followed was of Glock and McLean.

Study Design: Quantitative, cross sectional study. 

Settings: Institute of Biochemistry, Gulab Devi Educational Complex, Lahore

Duration: 01 Year i.e. 1st July 2020 to 30th June 2021.

Results: Enzymes activities of 6-PG dehydrogenase and Gluco-6- phospo dehydrogenase mentioned in table 1&2 in normal mammalian tissue and mammary glands. The results obtained on the tumour cells are given in table 3. These Values are within the limits in normal tissues whereas it becomes on higher side in lymphomas and sarcomas.

Conclusion: This study shows some limitation that the maximum enzymic activities are determined, whereas in the intact cell other regulatory factors probably limit or control the activity of this pathway.

Keywords: Gluco-6- phospodehydrogenase, 6-PG dehydrogenase, oxidative pathway, Ribose 5-Pentose, mammalian tissue