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Raman and resonance-Raman scattering by erythrocyte ghosts

Biochim Biophys Acta. 1975 Apr 8;382(4):542-51. doi: 10.1016/0005-2736(75)90221-7.

Abstract

1. We present the laser-Raman spectra of human erythrocyte ghosts, isolated by standard conditions and compare these with the spectra of lecithin liposomes and fat-free serum albumin. 2. The hydrocarbon stretching modes of membrane lipids are temperature sensitive and may serve as a index of hydrocarbon chain motion. 3. The Amide I and Amide III bands of ghosts in H-2O and 2-H-2O, indicate a mixture of alpha-helical and unordered conformation, but do not allow a quantitative estimate of secondary structure. 4. Strong, scattering bands at 1530 and 1165 cm-1 are attributable to conjugated double bond systems, probably of membrane-associated carotenoids. Their high intensity is due to resonance enhancement.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cattle
  • Cell Membrane / ultrastructure*
  • Choline / analysis
  • Egg Yolk
  • Erythrocytes / ultrastructure*
  • Female
  • Hot Temperature
  • Humans
  • Hydrogen-Ion Concentration
  • Lasers
  • Liposomes
  • Molecular Conformation
  • Phosphatidylcholines
  • Protein Conformation
  • Scattering, Radiation
  • Serum Albumin, Bovine
  • Spectrometry, Fluorescence
  • Spectrum Analysis

Substances

  • Liposomes
  • Phosphatidylcholines
  • Serum Albumin, Bovine
  • Choline