Laser raman spectroscopy of arylsulphatase B from rat liver.
1. The Raman spectra of native and denatured arylsulphatase B in aqueous solutions are reported. 2. Acid denaturation in 1 M-HCl solution (pH 1.2) was observed 1, 4 and 24 h after dissolution of the enzyme. 3. Changes in the geometry of the disulphide bridges and unfolding of the protein coil were observed. The observed decrease in the intensity of the tyrosine peaks indicates that these amino acid residues were shifted out.
D000818:Animals; D002803:Chondro-4-Sulfatase / Q000032:analysis* / Q000302:isolation & purification; D006851:Hydrochloric Acid / Q000494:pharmacology; D007834:Lasers; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008247:Lysosomes / Q000201:enzymology*; D008968:Molecular Conformation; D051381:Rats; D012996:Solutions; D013059:Spectrum Analysis, Raman / Q000379:methods; D013429:Sulfatases / Q000032:analysis*
D012996:Solutions; D013429:Sulfatases; D002803:Chondro-4-Sulfatase; D006851:Hydrochloric Acid