[Mixed "n" type inhibition of alpha-glucosidase activity by glucose in hemolymph of honeybee prenymphs].

Under in vitro inhibition of alpha-glucosidasic activity by glucose in hemolymph of Bee prenymphas, the reaction order (n) (predetermined according to the initial natural glycemia) decreases with increasing inhibitor concentration and the affinity constant between enzyme and substrate undergoes lower variations than in other cases where (n) does not change. The study of inhibited molecular forms suggests the possibility of a gradual negative-cooperativity mechanism concerning a dimeric form of the enzyme.