PYRUVATE METABOLISM AND CONTROL: FACTORS AFFECTING PYRUVIC CARBOXYLASE ACTIVITY.

Science (New York, N.Y.) ·Vol. 145 ·No. 3627 ·1964-07-03 ·Pages 58-60

FREEDMAN AD, KOHN L

Abstract

Pyruvic carboxylase activated by acetyl coenzyme A is highly active in the mitochondria of rodent liver, and its activity is increased in fasting and alloxan diabetes. In conjunction with acyl carboxylase activated by di- and tricarboxylic acid, it forms a reciprocating control network. Analog models of similar networks tend to correct for perturbations, stabilizing the overall system.

Keywords

ALLOXAN DIABETES AUTOMATIC DATA PROCESSING CARBON DIOXIDE CARBON ISOTOPES COENZYME A EXPERIMENTAL LAB STUDY FASTING INSULIN PROTAMINE ZINC LIGASES LIVER CYTOLOGY LIVER ENZYMOLOGY MICE MITOCHONDRIA PYRUVATES RATS TOXICOLOGIC REPORT

MeSH Terms

Animals Carbon Dioxide Carbon Isotopes Coenzyme A Diabetes Mellitus, Experimental Electronic Data Processing Fasting Insulin Insulin, Long-Acting Ligases Liver/cytology,enzymology Mice Mitochondria Protamines Pyruvates Pyruvic Acid Rats Research Toxicology

Chemicals

Carbon Isotopes Insulin Insulin, Long-Acting Protamines Pyruvates protamine zinc Carbon Dioxide Pyruvic Acid Ligases Coenzyme A

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

FREEDMAN A D

KOHN L

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.145.3627.58

Published

1964-07-03

Pages

58-60

Language

English

Region

United States

NLM ID

0404511

Subset

External Links

PubMed source DOI: 10.1126/science.145.3627.58 View journal details

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