TY - JOUR
T1 - Evidence for glycation of horse liver alcohol dehydrogenase in vivo
AU - Mcpherson, John Douglas
AU - Shilton, Brian H.
AU - Walton, Donald J.
PY - 1988/4/29
Y1 - 1988/4/29
N2 - A procedure involving HPLC of N-phenylthiocarbamyl derivatives of N-(1-deoxyhexitolyl)amino acids was used to show that borohydride-treated alcohol dehydrogenase, from horse liver, contained 0.16 mol of Nε-(1-deoxyhexitolyl) lysine per mol of enzyme. The identity of this compound was confirmed by mass spectrometry. It was concluded that glycation of alcohol dehydrogenase had occurred in vivo, resulting in the formation of Nε-(1-deoxyfructosyl) lysyl residues. The presence of the latter accounted for the retention of 14% of the enzyme by an agaroseboronate gel. These findings are interesting in view of the observation [Tsai, C. S., and White, J. H. (1983) Biochem. J. 209, 309-314] that the enzyme was activated when it was glycated in vitro.
AB - A procedure involving HPLC of N-phenylthiocarbamyl derivatives of N-(1-deoxyhexitolyl)amino acids was used to show that borohydride-treated alcohol dehydrogenase, from horse liver, contained 0.16 mol of Nε-(1-deoxyhexitolyl) lysine per mol of enzyme. The identity of this compound was confirmed by mass spectrometry. It was concluded that glycation of alcohol dehydrogenase had occurred in vivo, resulting in the formation of Nε-(1-deoxyfructosyl) lysyl residues. The presence of the latter accounted for the retention of 14% of the enzyme by an agaroseboronate gel. These findings are interesting in view of the observation [Tsai, C. S., and White, J. H. (1983) Biochem. J. 209, 309-314] that the enzyme was activated when it was glycated in vitro.
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U2 - 10.1016/S0006-291X(88)80096-2
DO - 10.1016/S0006-291X(88)80096-2
M3 - Article
C2 - 3365248
AN - SCOPUS:0024299346
VL - 152
SP - 711
EP - 716
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -