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A rice protein library: a data-file of rice proteins separated by two-dimensional electrophoresis

A rice protein library: a data-file of rice proteins separated by two-dimensional electrophoresis 122 86 86 8 8 S. Komatsu H. Kajiwara H. Hirano Department of Molecular Biology National Institute of Agrobiological Resources Kannondai, Tsukuba 305 Ibaraki Japan Abstract Proteins extracted from embryos, endosperms and leaves of rice were separated by two-dimensional electrophoresis and relative molecular weights and isoelectric points were determined. The separated proteins were electroblotted onto a polyvinylidene difluoride membrane and 85 electroblotted proteins were analyzed by a gas-phase protein sequencer. The N-terminal amino-acid sequences of 27 out of 85 proteins were determined in this manner. The N-terminal regions of the remaining proteins could not be sequenced and they were inferred to have a blocking group at the N-terminus. Among proteins, 11 could be sequenced after deblocking by in situ treatment with pyroglutamyl peptidase. The internal amino-acid sequences of 23 proteins were determined by sequence analysis of peptides obtained by Cleveland peptide mapping. The amino-acid sequences determined here were compared with those of known plant and animal proteins. The concanavalin A-peroxidase method was used to determine whether the 85 proteins were glycosylated and the diagonal electrophoresis method was used to determine whether they contained disulphide bonding. Finally, we constructed a data-file of rice proteins including information on relative molecular weight, isoelectric point, amino-acid sequence, sequence homology, glycosylation, and the presence of disulphide bonding. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png TAG Theoretical and Applied Genetics Springer Journals

A rice protein library: a data-file of rice proteins separated by two-dimensional electrophoresis

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References (29)

Publisher
Springer Journals
Copyright
Copyright © 1993 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Agriculture; Biochemistry, general; Plant Biochemistry; Plant Sciences; Plant Genetics & Genomics
ISSN
0040-5752
eISSN
1432-2242
DOI
10.1007/BF00211044
pmid
24194000
Publisher site
See Article on Publisher Site

Abstract

122 86 86 8 8 S. Komatsu H. Kajiwara H. Hirano Department of Molecular Biology National Institute of Agrobiological Resources Kannondai, Tsukuba 305 Ibaraki Japan Abstract Proteins extracted from embryos, endosperms and leaves of rice were separated by two-dimensional electrophoresis and relative molecular weights and isoelectric points were determined. The separated proteins were electroblotted onto a polyvinylidene difluoride membrane and 85 electroblotted proteins were analyzed by a gas-phase protein sequencer. The N-terminal amino-acid sequences of 27 out of 85 proteins were determined in this manner. The N-terminal regions of the remaining proteins could not be sequenced and they were inferred to have a blocking group at the N-terminus. Among proteins, 11 could be sequenced after deblocking by in situ treatment with pyroglutamyl peptidase. The internal amino-acid sequences of 23 proteins were determined by sequence analysis of peptides obtained by Cleveland peptide mapping. The amino-acid sequences determined here were compared with those of known plant and animal proteins. The concanavalin A-peroxidase method was used to determine whether the 85 proteins were glycosylated and the diagonal electrophoresis method was used to determine whether they contained disulphide bonding. Finally, we constructed a data-file of rice proteins including information on relative molecular weight, isoelectric point, amino-acid sequence, sequence homology, glycosylation, and the presence of disulphide bonding.

Journal

TAG Theoretical and Applied Genetics – Springer Journals

Published: Sep 1, 1993

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