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Biomedical subjects

W Kunz

Publications and source records attributed to W Kunz.

At least 163 records · Page 9Linked to original sources

Uber die beziehungen zwischen einem energieunabhängigen K(+)-H(+)-austausch und der strukturellen integrität von mitochondrien und membranpartikeln.

Disintegration or altering of intact mitochondria or digitonin inner membrane + matrix particles causes an increase in K(+)-linked release of protons. This effect is not obtainable in the case of outer membranes. It is assumed, that also the inner membrane + matrix possesses exchange sites for K(+), which are freely accessible for the potassium ion if the structural integrity is damaged. The outer layer of inner membrane seems to be a barrier for the K(+)-movement.

Journal Article↗

Uber die lokalisation eines energieunabhängigen K(+)-H(+)-austausches in der aussenmembran von rattenlebermitochondrien.

The energy-independent K(+)-H(+)-exchange was measured in intact mitochondria and submitochondrial particles at different K(+)-concentration of the incubation medium. Correlation was found between H+-displacement and specific activity of monoamine oxidase. It is concluded, that the energy-independent K(+)-H(+)-exchange is localized in the outer membrane of mitochondria.

Journal Article↗

Characterization of rapidly labelled rat liver ribonucleic acid showing high affinity for columns of methylated albumin on kieselguhr.

Most of the rapidly labelled RNA from rat liver submitted to column chromatography on methylated albumin on kieselguhr remains tightly bound to the column and can only be recovered by elution with m-ammonia. The tightly bound RNA is composed mainly of DNA-like RNA. The binding capacity is dependent not only on base composition but also on molecular size: the heavier RNA molecules show a greater affinity to the column than do the lower-molecular-weight components. Rapidly labelled mouse liver and Saccharomyces cerevisiae RNA show similar behaviour to rat liver RNA on columns of methylated albumin on kieselguhr.

Albumins↗