title: Viscometric characterization of pennisetin from pearl millet.
abstract: Pennisetin, the alcohol soluble storage protein of pearl millet (Pennisetum americanum), was isolated in a homogeneous state. The intrinsic viscosity [n] of this protein was found to be in the range of 16.5-17.7 ml/g in 70% (v/v) aqueous ethanol. The [eta] changed marginally when temperature was increased from 20 to 70 degrees C and also in the presence of 10 mM NaCl. The data indicated that pennisetin was a rigid, rod shaped asymmetric hydrodynamic particle with molecular dimensions in the range of 301 x 14.4 A - 317.7 x 14.2 A. During denaturation with guanidine hydrochloride (Gdn.HCl), the intrinsic viscosity of pennisetin increased from 16 to 25ml/g with a mid point at 3.6 M of the denaturant. The native protein structure was unfolded in 6 M Gdn.HCl as shown by the exposure of aromatic amino acid residues buried in the native state and this transition was found to be reversible. The intrinsic viscosity of pennisetin in 5.9 M Gdn.HCl corresponded to Mr 25,000 which was comparable to that determined by SDS-PAGE.
authors.affiliation: Division of Biochemical Sciences, National Chemical Laboratory, Pune, India.
authors.forename: M N
authors.initials: MN
authors.lastname: Sainani
authors.forename: A H
authors.initials: AH
authors.lastname: Lachke
authors.forename: N A
authors.initials: NA
authors.lastname: Sahasrabudhe
authors.forename: P K
authors.initials: PK
authors.lastname: Ranjekar
mesh_terms: D002523:Edible Grain / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D008897:Panicum / Q000737:chemistry*; D010940:Plant Proteins / Q000302:isolation & purification; D055315:Prolamins; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D014783:Viscosity
chemical_list: D010940:Plant Proteins; D055315:Prolamins