Abstract
myo-Inositol-1-phosphate synthase (EC 5.5.1.4) from rat testes, an NAD+-containing enzyme, which convertsd-glucose 6-phosphate to 1l-myo-inositol 1-phosphate, could be immobilized together with its cofactor and bovine serum albumin by crosslinking with glutaraldehyde at pH 4.5. The enzyme bound to the gel showed a specific activity of 5.6% of that of the native enzyme, but the activity could be increased to 21% by pretreatment with urea.

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