Journal of Lipid Research, Vol 19, 107-110, Copyright © 1978 by Lipid Research, Inc.
Labeling of high density lipoproteins with [3H] acetic anhydride
JB Marsh
Rat serum HDL was labeled by reaction with [3H] acetic anhydride at pH 7.2
for 30 min at room temperature by a modification of the method of Montelaro
and Rueckert (1975. J. Biol. Chem. 250: 1413). Protein specific activities
of 60 dpm/ng were achieved. Seven percent of the label was in lipid, of
which 92 percent was recovered in phospholipid. The labeled HDL migrated as
a single band as seen by electrophoretic or column chromatographic
analysis. When the labeled HDL was injected into rats without re-isolation,
the biological half-life was not significantly different from HDL labeled
in vitro with 125I or in vivo with amino acids. All of the apoproteins were
labeled; their specific activities were closer to one another than those
obtained with 125I. For some applications, acetylation may provide a useful
alternative to the 125I labeling procedure.