Abstract
A direct correlation exists between the ability of various N-aminoacylglucosamine derivatives (propionyl, butyryl, hexanoyl and octanoyl) to inhibit the four mammalian hexokinase isoenzymes and yeast hexokinase in free solution and their effectiveness as affinity chromatographic media for these enzymes when immobilized to Sepharose. Thus, by using Sepharose conjugates with different spacer molecules and/or adjusting the final ligand concentration attached to the gel, glucosamine affinity matrices have been designed to purify specifically each isoenzyme on a large scale. Chromatography of vertebrate skeletal myosin on columns of immobilized actin or ADP has shown that these myosin preparations contian mixtures of symmetrical homodimer isoenzymes with respect tot he light chains, i.e. each head of the myosin molecule is identical and contains two different light chains. Functionally these homodimers differ in their ability to bind to actin.
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