Peptide mapping and assessment of cryoprotective activity of 26/27-kDa dehydrin from soybean seeds.
To characterize the molecular weight diversity of seed dehydrin among soybean cultivars, 26/27-kDa soybean dehydrins were purified and compared in peptide mapping patterns, partial amino acid sequences, and cryoprotective activity on enzyme. In reverse phase chromatograms of their trypsin digests, we detected several distinctive peaks, one of which was attributed to a part of the internal glycine-rich region. Partial amino acid sequences of peptide fragments from trypsin and S. aureus V8 protease cleavage were found to be identical to the Mat9 translation. The CP50 of purified 26/27-kDa dehydrins were estimated to be 0.30 and 0.11 microM, respectively.
Momma
Michiko
M
National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. michiko@affrc.go.jp
Kaneko
Shigenobu
S
Haraguchi
Kazutomo
K
Matsukura
Ushio
U
D000595:Amino Acid Sequence; D000818:Animals; D003451:Cryoprotective Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D010449:Peptide Mapping; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology*; D011817:Rabbits; D012639:Seeds / Q000737:chemistry; D013025:Glycine max / Q000737:chemistry*
D003451:Cryoprotective Agents; D006360:Heat-Shock Proteins; D010446:Peptide Fragments; D010940:Plant Proteins; C070556:dehydrin proteins, plant; D007770:L-Lactate Dehydrogenase