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粪链球菌钠-ATP酶组分从膜上的释放。

Release of the component of Streptococcus faecalis Na(+)-ATPase from the membranes.

作者信息

Kakinuma Y, Igarashi K

机构信息

Faculty of Pharmaceutical Sciences, Chiba University, Japan.

出版信息

FEBS Lett. 1990 Oct 1;271(1-2):102-5. doi: 10.1016/0014-5793(90)80382-s.

Abstract

The Na(+)-stimulated ATPase activity of Streptococcus faecalis was lost by washing the membranes with ethylenediaminetetraacetic acid (EDTA). ATPase activities of both the EDTA extract and the stripped membranes did not show any stimulation by Na+ ions. However, the Na(+)-stimulated ATPase was readily reconstituted by an incubation of these fractions combined. It was only reconstituted from the fractions prepared under the condition that the Na(+)-ATPase is amplified, and not from those boiled or digested by trypsin. Thus, the component of Na(+)-ATPase of this organism is capable of being released from the membranes.

摘要

用乙二胺四乙酸(EDTA)洗涤粪链球菌的细胞膜后,其Na⁺刺激的ATP酶活性丧失。EDTA提取物和脱膜后的ATP酶活性均未表现出受Na⁺离子刺激。然而,将这些组分一起孵育时,Na⁺刺激的ATP酶很容易重新构成。它仅从在Na⁺-ATP酶被扩增的条件下制备的组分中重新构成,而不是从经煮沸或胰蛋白酶消化的组分中重新构成。因此,该生物体的Na⁺-ATP酶组分能够从细胞膜中释放出来。

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