title: Identification of lysine (384) in cytochrome P-450 LM2 as functionally linked residue.
abstract: Fluorescein isothiocyanate was selectively bound to the epsilon-amino group of a lysine residue of cytochrome P-450 LM2 at rho H 8.15. The decrease in the N-demethylase activity after modification evidences the functional importance of the modified group. After tryptic digestion the FITC-labeled peptide was isolated by means of HPLC and its amino acid composition determined. It was shown that the FITC-peptide can be attributed to the sequence Gly (379)- Arg (400) and that the label is selectively bound to Lys (384).
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis* / Q000302:isolation & purification; D016650:Fluorescein-5-isothiocyanate; D005452:Fluoresceins; D005456:Fluorescent Dyes; D066298:In Vitro Techniques; D007700:Kinetics; D008239:Lysine / Q000032:analysis*; D008297:Male; D008862:Microsomes, Liver / Q000032:analysis*; D011817:Rabbits; D013861:Thiocyanates
chemical_list: D000596:Amino Acids; D005452:Fluoresceins; D005456:Fluorescent Dyes; D013861:Thiocyanates; D003577:Cytochrome P-450 Enzyme System; D016650:Fluorescein-5-isothiocyanate; D008239:Lysine