ABSTRACT
Aldolase and triose-phosphate isomerase [TPI] were prepared and purified from rabbit skeletal muscle by gel chromatographic methods. Molecular weight determination and subunit interaction were demonstrated by gel filtration experiments. Cross-linking of aldolase subunit and TPI subunit with glutaraldehyde was detected from the elution profile of sephadex G/200 column which equilibrated with known proteins. Chemical interaction of the lysyl residue of aldolase with different inhibitors such as acetyl chloride, benzoyl chloride, chloroacetic acid, acetic anhydride, thiourea, thioacetamide and bromo ethyl acetate can prevent the Schiff's base formation and may induce some conformational changes. These conformational changes near catalytic site of aldolase causing inhibition of its catalytic function