title: Unusual denaturation properties of vicilin from Cajanus cajan.
abstract: Pigeonpea (Cajanus cajan) vicilin (Mr 190 kD) holoprotein contains 2 subunits and the N-terminal amino acid sequence is Gly-Ala-Arg-Val-Asp-Gln-Glu for purified vicilin subunit 1 (Mr 72 kD) and Thr-Thr-Cys-Met-Glu-Ser-Gly for purified vicilin subunit 2 (Mr 57 kD). Circular dichroism spectra of vicilin indicate the occurrence of a predominant beta- pleated sheet structure. The fluorescence studies of vicilin reveal its unusual stability to 8 M urea and 6 M guanidine HCl.
authors.affiliation: Division of Biochemical Sciences, National Chemical Laboratory, (Maharashtra), India.
authors.forename: Y R
authors.initials: YR
authors.lastname: Mawal
authors.forename: M R
authors.initials: MR
authors.lastname: Mawal
authors.forename: P K
authors.initials: PK
authors.lastname: Ranjekar
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D007887:Fabaceae; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D010946:Plants, Medicinal; D011489:Protein Denaturation; D055314:Seed Storage Proteins; D013050:Spectrometry, Fluorescence
chemical_list: D046911:Macromolecular Substances; D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D055314:Seed Storage Proteins; C015575:vicilin protein, plant