title: Characterization of pearl millet prolamins.
abstract: We report the physical-chemical characterization of the major alcohol-soluble proteins present in seeds of pearl millet (Pennisetum glaucum) by SDS-PAGE, bidimensional gel electrophoresis, MALDI-TOF/MS and RP-HPLC. We demonstrate the presence of three major prolamins, called A-, B- and C-pennisetin with mass values around 27, 22 and 12 kDa, respectively. We present partial amino acid sequences of these major proteins, which should allow the posterior isolation of the respective genes.
authors.affiliation: Embrapa Cenargen, PO box 1273, Brasilia, Brasil.
authors.forename: Lucilia Helena
authors.initials: LH
authors.lastname: Marcellino
authors.forename: Carlos
authors.initials: C
authors.lastname: Bloch Junior
authors.forename: Eugen Silvano
authors.initials: ES
authors.lastname: Gander
mesh_terms: D000595:Amino Acid Sequence; D002845:Chromatography; D002851:Chromatography, High Pressure Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry; D006109:Poaceae / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D010940:Plant Proteins