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INORGANIC PYROPHOSPHATASE OF RAT LIVER MITOCHONDRIA : Correlation of Latency with Catalytic Properties and Intramitochondrial Location
Stimulation of Mg(2+)-dependent inorganic pyrophosphatase activity several fold by disruption of mitochondrial membranes does not appreciably alter the catalytic properties of the enzyme. Stimulation is due to increased accessibility of substrate to the enzyme, which is not solublized on activation....
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1969
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2107579/ https://www.ncbi.nlm.nih.gov/pubmed/4306787 |
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author | Schick, Lloyd Butler, Larry G. |
author_facet | Schick, Lloyd Butler, Larry G. |
author_sort | Schick, Lloyd |
collection | PubMed |
description | Stimulation of Mg(2+)-dependent inorganic pyrophosphatase activity several fold by disruption of mitochondrial membranes does not appreciably alter the catalytic properties of the enzyme. Stimulation is due to increased accessibility of substrate to the enzyme, which is not solublized on activation. The enzyme is attached to the inside of the inner membrane, and under physiological conditions probably hydrolyzes only intramitochondrially-produced PP(i). |
format | Text |
id | pubmed-2107579 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1969 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21075792008-05-01 INORGANIC PYROPHOSPHATASE OF RAT LIVER MITOCHONDRIA : Correlation of Latency with Catalytic Properties and Intramitochondrial Location Schick, Lloyd Butler, Larry G. J Cell Biol Article Stimulation of Mg(2+)-dependent inorganic pyrophosphatase activity several fold by disruption of mitochondrial membranes does not appreciably alter the catalytic properties of the enzyme. Stimulation is due to increased accessibility of substrate to the enzyme, which is not solublized on activation. The enzyme is attached to the inside of the inner membrane, and under physiological conditions probably hydrolyzes only intramitochondrially-produced PP(i). The Rockefeller University Press 1969-07-01 /pmc/articles/PMC2107579/ /pubmed/4306787 Text en Copyright © 1969 by The Rockefeller University Press. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Schick, Lloyd Butler, Larry G. INORGANIC PYROPHOSPHATASE OF RAT LIVER MITOCHONDRIA : Correlation of Latency with Catalytic Properties and Intramitochondrial Location |
title | INORGANIC PYROPHOSPHATASE OF RAT LIVER MITOCHONDRIA : Correlation of Latency with Catalytic Properties and Intramitochondrial Location |
title_full | INORGANIC PYROPHOSPHATASE OF RAT LIVER MITOCHONDRIA : Correlation of Latency with Catalytic Properties and Intramitochondrial Location |
title_fullStr | INORGANIC PYROPHOSPHATASE OF RAT LIVER MITOCHONDRIA : Correlation of Latency with Catalytic Properties and Intramitochondrial Location |
title_full_unstemmed | INORGANIC PYROPHOSPHATASE OF RAT LIVER MITOCHONDRIA : Correlation of Latency with Catalytic Properties and Intramitochondrial Location |
title_short | INORGANIC PYROPHOSPHATASE OF RAT LIVER MITOCHONDRIA : Correlation of Latency with Catalytic Properties and Intramitochondrial Location |
title_sort | inorganic pyrophosphatase of rat liver mitochondria : correlation of latency with catalytic properties and intramitochondrial location |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2107579/ https://www.ncbi.nlm.nih.gov/pubmed/4306787 |
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