THE TOPOCHEMISTRY OF MEMBRANA FORM OF ALDEHYDE DEHYDROGENASE OF ERYTHROCYTES OF HUMAN BLOOD
Activity and kinetic characteristics of aldehyde dehydrogenase in fractions of erythrocytes of human blood were analyzed. Topochemistry of supramolecular forms of the enzyme has been discovered. Conducted investigation showed that most activity of aldehyde dehydrogenase prevails in the «shadows» of erythrocytes, which are membrane cell data. An affinity for substrates of reaction and catalytic efficacy of membrane aldehyde dehydrogenase higher than enzyme in matrix and gemolizate of erythrocytes has been established. Results of solubilization showed that membrane form of aldehyde dehydrogenase is heterogeneous and represented active and connected forms. Removal of part of the enzyme from erythrocyte membrane, affinity of the aldehyde dehydrogenase for substrates of reaction in the «shadows» of erythrocytes grows. Received data play essential significance for the regulation of this enzyme of biotransformation in the cell.