作者: M. S. Chauhan , M. B. Anand-Srivastava , V. Panagia , N. S. Dhalla
DOI: 10.1007/978-1-4899-5561-6_32
关键词:
摘要: The adenylate cyclase and Na+ -K+ ATPase activities decreased on storage at 4 degrees C as well freezing thawing of the rat heart sarcolemma. Treatment sarcolemmal fraction with phospholipase trypsin also depressed activities; was more sensitive to these treatments than cyclase. When enzyme were determined in presence different concentrations some cations activity enhanced by monovalent (Na+, K+, Rb+, Cs+, Li+, NH+4). Divalent such Sr2+, Ba2+, Co2+, Mn2+ had biphasic or no effects but inhibited activity. Although Ca2+, Ni2+, Cd2+, Cu2+, Hg2+, Zn2+ both activities, degree inhibition enzymes different. These results reveal role membrane integrity for full expression whereas divalent appear regulate sarcolemma-bound activities.