Molecular and kinetic properties of lactate dehydrogenase in the degenerating peripheral nerve

Abstract Electrophoretic and catalytic studies have been carried out on lactate dehydrogenase of normal and transected sciatic nerves of the rat. Lactate dehydrogenase of the intact nerve exhibits an almost even distribution of activity among its component iso-enzymes. The complete transection of the nerve is responsible for a deep and immediate shift of the enzyme towards the so-called muscle type pattern. Seven days after the nerve section the percentage activity of iso-enzyme 5 is almost three times higher than in the intact nerve. After a short lag period lactate dehydrogenase specific activity (activity/mg protein) undergoes a sharp decrease in transected nerves. The return of the elec…

LACTATE DEHYDROGENASE ISOENZYMES IN THE NERVOUS TISSUE?V..