Specificity and inhibition of an amylase present in the testicular tissue of the rat

Abstract

A carbohydrase is present in testicular tissue of normal rats, most being found in the soluble fraction of the tissue homogenate. The enzyme hydrolysed starch to maltose and maltotriose, indicating an endo-type amylase. It hydrolysed glycogen, but not maltose, isomaltose, panose and α-limit dextrins. Nitrofuranfuradroxyl, which causes spermatogenic arrest in the rat, inhibited the amylase activity of testicular tissue. In the seminiferous tubules, there was a decrease in the number of sperms and a gradual reduction in enzyme activity measured at early stages of spermatogenic arrest. Another abnormality was the formation of giant nuclei 23. When the enzyme of the treated animals was incubated in vitro, it hydrolysed starch into glucose in addition to the two normal products. Inhibition was of the competitive type; at substrate concentrations below 35 mg ml the K m was changed from 1.25 · 10 −4 M for the untreated to 4.3 · 10 −4 M for the treated enzyme in vitro. The activity of the in vitro-treated and untreated enzymes was decreased by dialysis. Addition of calcium chloride restored the activity of the untreated enzyme only. The inhibition in vivo was reversed only weeks after the removal of the furadroxyl.