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Interaction between phosphofructokinase and aldolase from Saccharomyces cevisiae studied by aqueous two-phase partitioning

Matic, Sandra LU ; Widell, Susanne LU ; Åkerlund, Hans-Erik LU and Johansson, Göte (2001) In Journal of Chromatography. B, Biomedical Sciences and Applications 751(2). p.341-348
Abstract
Phosphofructokinase (EC 2.7.1.11) and aldolase (EC 4.1.2.13) have been highly purified from Saccharomyces cerevisiae

by improved protocols. Partitioning of the enzymes in aqueous polymer two-phase systems was used to detect complex

formation. The partition of each enzyme was found to be affected by the presence of the other enzyme. AMP affected the

partition of the individual enzymes as well as the mixture of the two. The activities of the respective enzymes were

stimulated in the putative complex in an AMP-dependent manner. Two strictly conserved residues belonging to an acidic

surface loop of class II aldolases, are a potential site for electrostatic interaction with the positively charged... (More)
Phosphofructokinase (EC 2.7.1.11) and aldolase (EC 4.1.2.13) have been highly purified from Saccharomyces cerevisiae

by improved protocols. Partitioning of the enzymes in aqueous polymer two-phase systems was used to detect complex

formation. The partition of each enzyme was found to be affected by the presence of the other enzyme. AMP affected the

partition of the individual enzymes as well as the mixture of the two. The activities of the respective enzymes were

stimulated in the putative complex in an AMP-dependent manner. Two strictly conserved residues belonging to an acidic

surface loop of class II aldolases, are a potential site for electrostatic interaction with the positively charged regions close to

the active site in phosphofructokinase. Ó 2001 Elsevier Science B.V. All rights reserved. (Less)
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type
Contribution to journal
publication status
published
subject
in
Journal of Chromatography. B, Biomedical Sciences and Applications
volume
751
issue
2
pages
341 - 348
publisher
Elsevier
external identifiers
  • scopus:0035946025
ISSN
1387-2273
DOI
10.1016/S0378-4347(00)00492-8
language
English
LU publication?
yes
id
cbc53305-3af6-46c6-8549-44e08ce48ca0 (old id 1474808)
date added to LUP
2009-09-29 18:00:46
date last changed
2018-09-30 04:07:55
@article{cbc53305-3af6-46c6-8549-44e08ce48ca0,
  abstract     = {Phosphofructokinase (EC 2.7.1.11) and aldolase (EC 4.1.2.13) have been highly purified from Saccharomyces cerevisiae<br/><br>
by improved protocols. Partitioning of the enzymes in aqueous polymer two-phase systems was used to detect complex<br/><br>
formation. The partition of each enzyme was found to be affected by the presence of the other enzyme. AMP affected the<br/><br>
partition of the individual enzymes as well as the mixture of the two. The activities of the respective enzymes were<br/><br>
stimulated in the putative complex in an AMP-dependent manner. Two strictly conserved residues belonging to an acidic<br/><br>
surface loop of class II aldolases, are a potential site for electrostatic interaction with the positively charged regions close to<br/><br>
the active site in phosphofructokinase. Ó 2001 Elsevier Science B.V. All rights reserved.},
  author       = {Matic, Sandra and Widell, Susanne and Åkerlund, Hans-Erik and Johansson, Göte},
  issn         = {1387-2273},
  language     = {eng},
  number       = {2},
  pages        = {341--348},
  publisher    = {Elsevier},
  series       = {Journal of Chromatography. B, Biomedical Sciences and Applications},
  title        = {Interaction between phosphofructokinase and aldolase from Saccharomyces cevisiae studied by aqueous two-phase partitioning},
  url          = {http://dx.doi.org/10.1016/S0378-4347(00)00492-8},
  volume       = {751},
  year         = {2001},
}