Comparison of activities of several enzymes and protein constituents of oviducal and breast muscle of Japanese quail, Coturnix coturnix Japonica

Abstract

1. 1. Activities of several enzymes and protein constituents of magnum, isthmus, shell gland and breast muscle (pectoralis major) of Japanese quail, Coturnix coturnix japonica were compared. 2. 2. The respective activity per g wet weight of lactate dehydrogenase, malate dehydrogenase and l-glycerol 3-phosphate dehydrogenase in pectoralis major was approx 20 times that of these enzymes in isthmus which showed the highest activity among oviducal tissues. On the other hand, the respective activity of lactate dehydrogenase was similar to that of malate dehydrogenase and was approx 10–20 times that of l-glycerol 3-phosphate dehydrogenase in each tissue. 3. 3. Among NADPH-producing enzymes, NADP +-isocitrate dehydrogenase showed the highest activity in all tissues. The activity of malic enzyme was lowest in oviducal tissues, but was next to NADP +-isocitrate dehydrogenase in pectoralis major. 4. 4. Sodium dodecyl sulfate polyacrylamide gel electrophoretic patterns of the whole homogenate, the supernatant and the precipitate fraction of magnum, isthmus, shell gland and pectoralis major showed tissue specific protein compositions. Proteins with molecular weight of 55,000, 70,000, 110,000 and 130,000 were observed in the respective precipitate (myofibrilar) fraction of magnum, isthmus and shell gland, but not in that of pectoralis major. It was noteworthy that the amount of myosin heavy chain of magnum was markedly less than that of other three tissues.