Two-dimensional electrophoresis of plant proteins and standardization of gel patterns.
Proteins of two plants, Arabidopsis thaliana and rice (Oryza sativa) were subjected to two-dimensional electrophoresis analysis with two modifications: (i) comigration of external standard marker proteins with resultant horizontal and vertical stripes in the gel, and (ii) deblocking with a vapor of aqueous heptafluorobutyric acid for N-acetylserine. Approximately 5000 protein spots were separated from both the five tissues of Arabidopsis and the nine tissues of rice. Over one hundred spots were electroblotted for N-terminal sequencing. Among the newly sequenced proteins, 62 were from Arabidopsis and 51 from rice.
Tsugita
A
A
Research Institute for Biosciences, Science University of Tokyo, Noda, Japan.
Kamo
M
M
Kawakami
T
T
Ohki
Y
Y
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D008969:Molecular Sequence Data; D012275:Oryza / Q000378:metabolism*; D010940:Plant Proteins / Q000032:analysis*; D012015:Reference Standards
D010940:Plant Proteins