MARC details
000 -LEADER |
fixed length control field |
02323nam a22002897a 4500 |
003 - CONTROL NUMBER IDENTIFIER |
control field |
ZW-GwMSU |
005 - DATE AND TIME OF LATEST TRANSACTION |
control field |
20250307121454.0 |
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION |
fixed length control field |
250307b |||||||| |||| 00| 0 eng d |
040 ## - CATALOGING SOURCE |
Original cataloging agency |
MSU |
Language of cataloging |
English |
Transcribing agency |
MSU |
Description conventions |
rda |
050 00 - LIBRARY OF CONGRESS CALL NUMBER |
Classification number |
QK711.2 JOU |
100 1# - MAIN ENTRY--PERSONAL NAME |
Personal name |
Eprintsev, Alexander T |
Relator term |
author |
245 10 - TITLE STATEMENT |
Title |
Expression and properties of the mitochondrial and cytosolic forms of aconitase in maize scutellum |
Statement of responsibility, etc. |
created by Alexander T Eprintsev, Dmitry N Fedorin, Marina V Nikitina and, Abir U Igamberdiev |
264 1# - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE |
Place of production, publication, distribution, manufacture |
Amsterdam: |
Name of producer, publisher, distributor, manufacturer |
Elsevier GmbH, |
Date of production, publication, distribution, manufacture, or copyright notice |
2015. |
336 ## - CONTENT TYPE |
Source |
rdacontent |
Content type term |
text |
Content type code |
txt |
337 ## - MEDIA TYPE |
Source |
rdamedia |
Media type term |
unmediated |
Media type code |
n |
338 ## - CARRIER TYPE |
Source |
rdacarrier |
Carrier type term |
volume |
Carrier type code |
nc |
440 ## - SERIES STATEMENT/ADDED ENTRY--TITLE |
Title |
Journal of palnt physiology |
Volume/sequential designation |
Volume 181 |
520 3# - SUMMARY, ETC. |
Summary, etc. |
Aconitase (EC 4.2.1.3) catalyzes the reversible interconversion of citrate, cis-aconitate, and D-isocitrate. It operates in mitochondria and cytosol. We investigated the expression of two aconitase genes (Aco1 and Aco4) and activities of the mitochondrial and cytosolic forms in maize (Zea mays L.) scutellum during germination. Both forms were isolated and purified. The cytosolic form had a higher pH optimum (8.0), twice higher affinity to citrate (K(m) 9.5 mM), and slightly lower affinity to D,L-isocitrate (K(m) 1.7 mM) as compared to the mitochondrial form (optimum pH 7.5, K(m) with citrate 21 mM, and K(m) with isocitrate 1.5 mM). The highest activity of both forms of aconitase was observed on the 4th day of germination; then the activity and expression of the cytosolic form sharply decreased, while the mitochondrial form decreased more slowly. The mitochondrial aconitase was more strongly inhibited by H2O2 (half-inhibition at 35 μM) than the cytosolic form (60 μM). Aconitase activity was not detected in the glyoxysomal fraction beyond the cross-contamination level. It is suggested that the mitochondrial form operates in the tricarboxylic acid cycle, whereas the cytosolic form participates in the reactions of the glyoxylate cycle taking place outside the glyoxysome. |
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
Topical term or geographic name entry element |
Aconitase |
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
Topical term or geographic name entry element |
Glyoxylate cycle |
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
Topical term or geographic name entry element |
Mitochondria |
700 1# - ADDED ENTRY--PERSONAL NAME |
Personal name |
Fedorin, Dmitry N |
Relator term |
co-author |
700 1# - ADDED ENTRY--PERSONAL NAME |
Personal name |
Nikitina, Marina V |
Relator term |
co-author |
700 1# - ADDED ENTRY--PERSONAL NAME |
Personal name |
Igamberdiev, Abir U |
Relator term |
co-author |
856 ## - ELECTRONIC LOCATION AND ACCESS |
Uniform Resource Identifier |
https://doi.org/10.1016/j.jplph.2015.03.012 |
942 ## - ADDED ENTRY ELEMENTS (KOHA) |
Source of classification or shelving scheme |
Library of Congress Classification |
Koha item type |
Journal Article |