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. 1985 Sep 15;41(9):1149-51.
doi: 10.1007/BF01951702.

Immobilization of chicken liver fructose 1,6-bisphosphatase on CNBr-activated Sepharose

G Y Han, Y H Wang, H C McBay, J Johnson, P F Han

Immobilization of chicken liver fructose 1,6-bisphosphatase on CNBr-activated Sepharose

G Y Han et al. Experientia. .

Abstract

Chicken liver fructose 1,6-bisphosphatase is readily immobilized on CNBr-activated Sepharose. The immobilization alters some enzymatic properties. They include broader pH activity curve, loss of activation by K+ or NH+4, increased resistance to inactivation by trypsin, decreased sensitivity to AMP inhibition, and loss of cooperative interaction among AMP-binding sites. The immobilized enzyme retains about 38% or 19% of the specific activity of the native enzyme when the activity is measured in the absence or presence of K+, respectively.

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