Interconvertible Forms of Glycogen Phosphorylase in Neurospora crassa

Glycogen phosphorylase in extracts of N. crassa mycelia has two interconvertible forms: one active (a form) and the other inactive (b form) in the absence of 5′-AMP. The conversion of the b to the a form requires ATP- Mg2+ and proceeds at higher rate in the presence of 3′,5′-cyclic AMP.

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Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 66; no. 2; pp. 459 - 463
Main Authors Téllez-Iñón, María T., Torres, Héctor N.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 01.06.1970
National Acad Sciences
Subjects
Adenine Nucleotides - metabolism
Adenosine Triphosphate - metabolism
Biochemistry
Biological Sciences: Biochemistry
Centrifugation
Cyclic AMP - pharmacology
Enzyme preparations
Enzymes
Glucose - pharmacology
Glucosyltransferases - metabolism
Glycogen
Metabolism
Neurospora - enzymology
Phosphates - pharmacology
Quaternary ammonium compounds
Sulfates
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Summary:Glycogen phosphorylase in extracts of N. crassa mycelia has two interconvertible forms: one active (a form) and the other inactive (b form) in the absence of 5′-AMP. The conversion of the b to the a form requires ATP- Mg2+ and proceeds at higher rate in the presence of 3′,5′-cyclic AMP.
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Career investigator of the Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina), and to whom requests for reprints should be sent.
Supported by a grant of the Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina).
This work was supported by grants from the U.S. Public Health Service (GM 03442) and the Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina).
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.66.2.459