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Isolation of membrane-bound renal enzymes that metabolize kinins and angiotensins

机译:膜结合肾酶的分离,即代谢Kinins和血管紧张素

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pCortex of rat kidney was homogenized and fractions enriched in plasma membrane, endoplasmic reticulum or brush border were prepared by several techniques of differential centrifugation. The identity and homogeneity of the membrane fragments were investigated by assaying marker enzymes and by transmission and scanning electron microscopy. Kallikrein was present in both plasma-membrane- and endoplasmic-reticulum-enriched fractions isolated by two fractionation procedures. Kallikrein was highly concentrated in a plasma-membrane fraction but was absent from the brush-border membrane of proximal tubular cells. Cells of transplanted renal tumours of the rat, originating from the proximal tubule, had no kallikrein activity. Kininase activity, angiotensin I-converting enzyme (kininase II) and angiotensinase were found in a plasma-membrane-enriched fraction and especially in the fraction containing isolated brush border. It is suggested that after renal kallikrein is synthesized on endoplasmic reticulum, it is subsequently reoriented to a surface membrane for activation and release. Renal kallikrein may enter the tubular filtrate distal to the proximal tubules. The brush-border membrane of proximal tubule is the major site of inactivation of kinins and angiotensin II../p
机译:>大鼠肾的皮质是均质化的,并通过几种差分离心技术制备富含质膜,内质网或刷子边界的级分。通过测定标记酶和透射电子显微镜来研究膜片段的同一性和均匀性。 Kallikrein以两种分馏方法分离的血浆膜和内质 - 网状型富集的级分存在。 Kallikrein高度浓缩,膜膜馏分高,但不存在近端管状细胞的刷边膜。大鼠移植肾肿瘤的细胞,来自近端小管,没有Kallikrein活性。激素酶活性,血管紧张素I-转换酶(激酶II)和血管紧张素酶在富含血浆膜富集的级分中发现,特别是在含有隔离刷边界的级分中。建议在成内质网上合成肾kallikrein后,随后将其重新定向到用于活化和释放的表面膜。肾kallikrein可以进入远端小管的管状滤液。近端小管的刷界膜是Kinins和血管紧张素II灭活的主要部位..

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