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Changes in protein synthesis in embryonic axes after long-term storage of maize seeds

Published online by Cambridge University Press:  19 September 2008

R. Aguilar ,
E. Reynoso ,
M. Albores  and
E. Sánchez de Jiménez
R. Aguilar
Affiliation:
Department of Biochemistry, Facultad de Química, UNAM, Ciudad Universitaria, Mexico D F, 04510Mexico
E. Reynoso
Affiliation:
Department of Organic Chemistry, Facultad de Química, UNAM, Ciudad Universitaria, Mexico D F, 04510Mexico
M. Albores
Affiliation:
Department of Organic Chemistry, Facultad de Química, UNAM, Ciudad Universitaria, Mexico D F, 04510Mexico
E. Sánchez de Jiménez*
Affiliation:
Department of Biochemistry, Facultad de Química, UNAM, Ciudad Universitaria, Mexico D F, 04510Mexico
*
* Correspondence
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Abstract

The aim of this work was to analyse the capacity for protein synthesis in embryonic axes from long-term-stored maize seeds, including the role of proline. Embryonic axes from seeds stored for 13 years (S) and non-stored seeds (NS) were incubated in nutrient media after application of [14C]proline. Transformation of [14C]proline into other amino acids was analysed by thin-layer chromatography. After 6 h of incubation, no other labelled amino acids were found. Incorporation of 14C into total soluble and cell-wall (proline-rich) proteins was assessed during this period. Incorporation of [14C]proline into specific cell-wall proteins was lower in S than in NS axes.

Studies using [35S]methionine showed that protein synthesis was slower in axes of S than in NS seeds. Analyses of these proteins by gel electrophoresis and fluorography revealed qualitative differences between the [35S]methionine proteins synthesized by both types of axes. The NS: S ratios for the [35S]proteins were larger than those from the [14C]proline assays. These data may be interpreted as an indication of differential deterioration of transcription or translation in the axes during long-term seed storage.

Keywords

prolineprotein synthesisseed storageZea mays
Type
Research Papers
Information
Seed Science Research , Volume 2 , Issue 4 , December 1992 , pp. 191 - 198
Copyright
Copyright © Cambridge University Press 1992

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