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Rat liver hexokinases during development.

The four glucose-phosphorylating isozymes from rat liver were separated by DEAE-cellulose column chromatography at several ages during development. The isozymes exhibited a sequential mode of appearance. The isozymes A, B, and C reached maximal values of activity at days +1, +3, and +7, respectively, decaying afterwards to the low characteristic adult value. Isozyme D activity was detected in very low levels as early as day +3, rising from day +18 to reach constant adult values at day +30. A fraction of the glucose phosphorylating activity was found associated with particulate material in prenatal and newborn rats. From day +15 onwards, no particulate activity could be detected. The particulate activity was found to be composed of three low-Km isozymes as of the corresponding soluble fraction.