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钠钾激活的ATP酶:体外解剖的兔肾单位节段中的活性成熟

Na-K-activated ATPase: activity maturation in rabbit nephron segments dissected in vitro.

作者信息

Schmidt U, Horster M

出版信息

Am J Physiol. 1977 Jul;233(1):F55-60. doi: 10.1152/ajprenal.1977.233.1.F55.

Abstract

Single, defined nephron segments were dissected in vitro from fresh slices of neonatal and mature rabbit kidney. Na-K-ATPase was quantified for six different tubule segments with an ultramicromethod. The enzyme distribution pattern in the neonatal nephron was similar to that in the mature nephron. Activity in distal segments was 2-5 times higher than proximal tubule activity referred to tissue dry weight, and 2 times higher referred to tubule length. Neonatal enzyme activity was lower than mature in all segments. Some segments carried only 23% of mature activity. Enzyme activity in the proximal convoluted tubule was constant during maturation when referred to the basal and lateral membrane area measured in the same developmental stages. In vitro activities of these tubules were similar to the enzyme activity measured previously in freeze-dried slices. The Vmax during development of Na-K-ATPase was higher by a factor of 5 in the mature tubule, whereas the Km was identical in the neonatal and mature tubule. The ouabain-insensitive ATPase did not show a maturational activity change.

摘要

从新生和成年兔肾脏的新鲜切片中体外分离出单个、明确的肾单位节段。采用超微量法对六个不同肾小管节段的钠钾ATP酶进行定量。新生肾单位中的酶分布模式与成年肾单位相似。以组织干重计,远曲小管节段的活性比近曲小管活性高2至5倍,以小管长度计则高2倍。所有节段的新生酶活性均低于成年期。有些节段的活性仅为成年期的23%。当以相同发育阶段测量的基底膜和侧膜面积计,近曲小管中的酶活性在成熟过程中保持恒定。这些肾小管的体外活性与先前在冻干切片中测得的酶活性相似。钠钾ATP酶在发育过程中的Vmax在成熟肾小管中高出5倍,而新生和成熟肾小管中的Km相同。哇巴因不敏感的ATP酶未显示出成熟活性变化。

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