Al. Trout et al., Direct capillary electrophoretic detection of carbohydrate-deficient transferrin in neat serum, ELECTROPHOR, 21(12), 2000, pp. 2376-2383
Transferrin, an iron transport protein found in serum and cerebrospinal flu
id, is known to be microheterogeneous with respect to its carbohydrate and
sialic acid content. The forms of transferrin deficient in sialic acid and/
or carbohydrate, termed carbohydrate-deficient transferrin (CDT), have been
of clinical interest for almost two decades as a result of the initial fin
ding that elevated CDT concentrations are associated with chronic, excessiv
e alcohol abuse. We demonstrate the utility of capillary electrophoresis fo
r examining the CDT sialoform profile via the direct electrophoresis of ser
um. The need for negligible preelectrophoresis sample preparation and absen
ce of postelectrophoresis processing dramatically decreases analysis time c
ompared to slab gel-based separations. Using a fluorocarbon-coated capillar
y containing a hydroxyethyl cellulose/ berate buffer, the high resolution s
eparation of serum components is effected in less than 30 min. Under these
conditions, the beta region proteins (including transferrin) are well resol
ved from the alpha-2 and gamma zone proteins in a window where the individu
al transferrin sialoforms can be detected. The usefulness of this method is
demonstrated with the electrophoresis of serum from subjects known to be e
ither nonalcoholic and alcoholic.