Salt-mediated interconversions and purification of malate synthase from germinating soybean cotyledons (Glycine max. L.)

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State: Public
Version: author
Serval ID
serval:BIB_19DEAFBBABE7
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Salt-mediated interconversions and purification of malate synthase from germinating soybean cotyledons (Glycine max. L.)
Journal
Plant Science
Author(s)
Henry H., Escher C.L., Widmer F.
ISSN
0168-9452
Publication state
Published
Issued date
1992
Peer-reviewed
Oui
Volume
82
Number
1
Pages
21-27
Language
english
Abstract
The effects of MgCl2 and KCl on the structural properties of malate synthase from germinating soybean (Glycine max. L). were investigated. The enzyme was obtained from isolated glyoxysomes or from crude homogenates. It was clearly shown to undergo reversible structural interconversions depending on ionic strength as adjusted by MgCl2 and KCl (membrane bound enzyme form, precipitable aggregates, soluble dimeric and decameric forms). These interconversions were taken advantage of in the purification procedure.
Keywords
MALATE SYNTHASE, SOYBEAN, GLYCINE-MAX, GERMINATION, CASTOR-BEAN ENDOSPERM, ENDOPLASMIC-RETICULUM, ENZYMES, MEMBRANE, MICROBODIES, PROTEINS, GLYOXYSOMES, ATPASE, CYCLE, CELLS
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Create date
13/08/2015 9:01
Last modification date
11/04/2020 7:08
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