Interaction between phosphofructokinase and aldolase from Saccharomyces cevisiae studied by aqueous two-phase partitioning
(2001) In Journal of Chromatography. B 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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1474808
- author
- Matic, Sandra LU ; Widell, Susanne LU ; Åkerlund, Hans-Erik LU and Johansson, Göte
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chromatography. B
- 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
- 2016-04-01 16:00:49
- date last changed
- 2022-01-28 08:44:17
@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}},
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}},
doi = {{10.1016/S0378-4347(00)00492-8}},
volume = {{751}},
year = {{2001}},
}