Proteome analysis of wheat lemma.
We report here for the first time on the construction of proteomes from wheat lemma at the anthesis stage. After transfer of lemma proteins to polyvinylidene difluoride membranes, seventy larger spots were subjected to peptide sequence analysis; the amino acid sequences could be described for forty-eight of these proteins. The result suggested that wheat proteins were less N-terminally blocked compared to rice proteins, which are known to have a much higher ratio of N-terminal blocks. We further analyzed the internal sequences of eight blocked proteins by the Cleveland peptide mapping method. Out of these total 56 amino acid sequences, forty-one could be assigned to the corresponding expressed sequence tags (ESTs). The expression profile of lemma proteins was generally similar to that of leaf, and the majority of identified proteins were related to cellular metabolisms. We analyzed the internal sequences of one protein spot present in lemma, which was not present in leaf.
Woo
Sun-Hee
SH
Laboratory for Remediation Research, Plant Science Center, RIKEN, Wako, Saitama, Japan.
Kimura
Makoto
M
Higa-Nishiyama
Arisa
A
Dohmae
Naoshi
N
Hamamoto
Hiroshi
H
Jong
Seung-Keun
SK
Yamaguchi
Isamu
I
D000595:Amino Acid Sequence; D015180:Electrophoresis, Gel, Two-Dimensional; D035264:Flowers / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010940:Plant Proteins / Q000302:isolation & purification*; D020543:Proteome; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism; D014908:Triticum / Q000737:chemistry*
D010446:Peptide Fragments; D010940:Plant Proteins; D020543:Proteome; D012273:Ribulose-Bisphosphate Carboxylase