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PMID: 6264456 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Fructose-bisphosphatase as a substrate of cyclic AMP-dependent protein kinase.

Hosey MM, Marcus F

Abstract

We have tested rat liver fructose-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) and three other gluconeogenic fructose-bisphosphatases as substrates for the catalytic subunit of cyclic AMP-dependent protein kinase. In contrast to the rat liver enzyme, homogeneous preparations of mouse liver, rabbit liver, and pig kidney fructose-bisphosphatase could not be phosphorylated by the kinase. Comparative sodium dodecyl sulfate/polyacrylamide gel electrophoresis of the four above fructose-bisphosphatases revealed that the subunit molecular weight of the isolated rat liver enzyme (ca. 40,000-42,000) was greater than that of mouse liver, rabbit liver, and pig kidney fructose-bisphosphatases (ca. 36,000-37,000). Treatment of 32P-labeled rat liver fructose-bisphosphatase with trypsin resulted in the conversion of the rat liver enzyme to an active species with a subunit molecular weight identical to that of the three other enzymes, with complete loss of the 32P-labeled site. Identical trypsin treatment of pig kidney fructose-bisphosphatase caused no change in the molecular weight of the enzyme. The results suggest that the purified mouse liver, rabbit liver, and pig kidney fructose-bisphosphatases are not substrates for the cyclic AMP-dependent protein kinase in vitro because they lack the phosphorylation-site peptide.

MeSH Terms
Animals Binding Sites Cyclic AMP/metabolism Fructose-Bisphosphatase/metabolism Kidney/enzymology Liver/enzymology Mice Peptide Fragments/metabolism Phosphorylation Protein Kinases/metabolism Rabbits Rats Substrate Specificity Swine Trypsin
Chemicals
Peptide Fragments Cyclic AMP Protein Kinases Fructose-Bisphosphatase Trypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hosey M M
Marcus F
References (24)
24 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1981-01-00
Pages
91-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC318996
Subset
IM
Grants
NIADDK NIH HHS · AM 21167 · United States
NHLBI NIH HHS · HL 23306 · United States
NCRR NIH HHS · RR 05366 · United States
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