The in vitro glycation of lysozyme and the influence of buffer concentration investigated by mass spectrometry.
The non-enzymatic reactions between glucose or fructose with lysozyme, performed under pseudo-physiological conditions, have been studied by means of matrix-assisted laser desorption/ionization mass spectrometry. Phosphate buffer at concentrations of 0.05, 0.2 and 0.5 M has been employed. The formation of glycated proteins as well as of cross-linking products has been always observed. In the case of glucose, high phosphate buffer concentrations affect the glycation kinetics and promote the formation of cross-linking products. With fructose, such influence is moderate, the reaction kinetics being mainly influenced by the higher reactivity of the sugar.
Lapolla
A
A
Istituto di Medicina Interna, Malattie del Metabolismo, Padova, Italy.
Fedele
D
D
Aronica
R
R
Baldo
L
L
D'Alpaos
M
M
Seraglia
R
R
Traldi
P
P
D002021:Buffers; D003432:Cross-Linking Reagents; D005632:Fructose / Q000737:chemistry; D005947:Glucose / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D010710:Phosphates / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D002021:Buffers; D003432:Cross-Linking Reagents; D010710:Phosphates; D005632:Fructose; D009113:Muramidase; D005947:Glucose