[大脑和肾脏中钠钾ATP酶同工酶的热敏感性]

[Thermal sensitivity of Na+,K+-ATPase isoenzymes in the brain and kidney].

作者信息

Kaplia A A, Kravtsov A V, Kravtsova V V

出版信息

Ukr Biokhim Zh (1978). 1994 Nov-Dec;66(6):58-66.

Abstract

Thermal stabilities of Na+, K(+)-ATP-ase preparations with different isozyme content from brain and kidneys of different animal species have been compared. The greater thermal lability of the alpha(+)-isoform of a catalytic subunit of Na+, K(+)-ATP-ase is established. The method of specific thermal inactivation of in brain preparations was used in comparative study of ouabain sensitivity of Na+, K(+)-ATP-ase isozymes from rat, cow and rabbit. It is concluded that the existing structural and functional model of the receptor site of Na+, K(+)-ATP-ase catalytic subunit is not sufficient for the complete explanation of the species heterogeneity of Na+, K(+)-ATP-ase affinity to heart glycosides.

摘要

已对来自不同动物物种大脑和肾脏的、具有不同同工酶含量的Na +，K(+)-ATP酶制剂的热稳定性进行了比较。确定了Na +，K(+)-ATP酶催化亚基的α(+)-同工型具有更高的热不稳定性。在对大鼠、牛和兔的Na +，K(+)-ATP酶同工酶哇巴因敏感性的比较研究中，采用了大脑制剂特异性热失活的方法。得出的结论是，Na +，K(+)-ATP酶催化亚基受体位点的现有结构和功能模型不足以完全解释Na +，K(+)-ATP酶对强心苷亲和力的物种异质性。