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[大鼠脑Na⁺,K⁺-ATP酶催化亚基同工型对Ds-Na的敏感性]

[Sensitivity of rat brain Na+,K+-ATPase catalytic subunit isoforms to Ds-Na].

作者信息

Kaplia A A, Kravtsov A V, Kravtsova V V

出版信息

Biokhimiia. 1995 Jun;60(6):970-5.

PMID:7654867
Abstract

Analysis of the detergent effect on the dose response curve of ouabain inhibition of rat brain Na+,K(+)-ATPase revealed that the microsomal alpha(+)-isoform was more stable to inactivation by SDS than the alpha-isoform of Na+,K(+)-ATPase from brain cortex and renal outer medulla. Data from SDS-PAAG electrophoresis of membrane-bound Na+,K(+)-ATPase suggest that irreversible inactivation of the isozymes is accompanied by their removal from the membrane but the alpha-isoform is more sensitive to the solubilizing effect of SDS.

摘要

对去污剂对哇巴因抑制大鼠脑Na +,K(+)-ATP酶剂量反应曲线的影响进行分析,结果显示微粒体α(+)同工型比来自脑皮质和肾外髓质的Na +,K(+)-ATP酶的α同工型对SDS失活更稳定。膜结合Na +,K(+)-ATP酶的SDS-PAAG电泳数据表明,同工酶的不可逆失活伴随着它们从膜上的去除,但α同工型对SDS的增溶作用更敏感。

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