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Journal ArticleDOI

Quantitative Histochemie am Nephron Oxydoreduktasen und Na K stimulierte ATPase.

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This article is published in Progress in Histochemistry and Cytochemistry.The article was published on 1971-01-01. It has received 43 citations till now. The article focuses on the topics: Na+/K+-ATPase.

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Enzyme distribution along the nephron

TL;DR: Drug metabolism, steroid hormone hydroxylations, renal gluconeogenesis as well as renal choline and triglyceride metabolism may be better understood by the knowledge of their precise localization along the nephron.
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Sites of enzyme activity along the nephron

TL;DR: The purpose of this review is to summarize some results obtained by the determination of enzymes of carbohydrate and energy metabolism in single portions of the rat nephron, and to discuss their possible relationships to renal transport processes.
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Quantitative morphology of the rat kidney

TL;DR: Light and electron microscopic morphometry was used to determine the volumetric tissue composition within the various zones of the rat kidney and a close correlation between the membrane bound enzymes cytochrome- c oxidation and Na-K-ATPase could be demonstrated for mercury induced renal injury.
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Sodium- and potassium-activated ATPase. A possible target of aldosterone.

TL;DR: It appears that this aldosterone effect on Na-K-ATPase requires an intact protein synthetic process and is completely prevented by actinomycin D and cycloheximide.
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Hydroxyproline metabolism by the rat kidney: Distribution of renal enzymes of hydroxyproline catabolism and renal conversion of hydroxyproline to glycine and serine

TL;DR: The results suggest that hydroxyproline degradation could contribute significantly to the renal synthesis of serine.
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Functions of lysosomes.

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Enzymatic basis for active transport of na+ and k+ across cell membrane.

J. C. Skou
TL;DR: Afhnity for Monovalent Cations and Quantitative Relation between Effect of Na+ + K+ on Enzyme System and Active Transport in Intact Cell.
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