Kaplia A A, Kravtsov A V
Ukr Biokhim Zh (1978). 1990 Jul-Aug;62(4):39-44.
Thermal stabilities of Na+,K(+)-ATPase isozymes from the rat brain and kidney tissues are compared. It is established that heat treatment of Na+,K(+)-ATPase preparations from the brain decreases the high affinity component of the ouabain inhibition of the enzyme activity due to selective inactivation of alpha-isoform. Its higher thermal lability in comparison with alpha-isoform is confirmed.
比较了大鼠脑和肾组织中Na +,K(+)-ATP酶同工酶的热稳定性。已确定,对来自大脑的Na +,K(+)-ATP酶制剂进行热处理会降低哇巴因对酶活性抑制的高亲和力成分,这是由于α同工型的选择性失活所致。证实了其与α同工型相比具有更高的热不稳定性。