Isolation and purification of phosphate dependent glutaminase from sarcoma-180 tumor and its antineoplastic effects on murine model system

High rate of glutamine use is a characteristic of tumor cell both in vivo a nd in vitro and experimental cancer therapies have developed by depriving t umor cells of glutamine, In several investigations, bacterial glutaminase w as found to be a potent therapeutic agent against varieties of tumor, but i t showed suppressive effects on haematopoietic systems and inhibitory effec ts on normal lymphocytic blastogenesis. No antineoplastic study has neverth eless been undertaken with glutaminase enzyme purified from mammalian sourc e. In the present study we report the purification of glutaminase enzyme fr om mitochondria of highly malignant S-180 cell using ion exchange chromatog raphy and affinity column chromatography of glutamine. Purified enzyme is a kidney type phosphate dependent glutaminase with Mr 64 KD. Effect of enzym e therapy has been investigated in transplantable as well as induced tumor model in both ascites and solid form, It has been observed that the enzyme at the total dose of 10 unit/mouse successfully inhibited the tumor burden both in ascitic and solid tumor and subsequently increases the host's life span. There was no significant toxic effect on the peripheral blood cells.