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Oak Ridge Poster Sessions |
1
Helena Labs., Beaumont, TX;
a author for
correspondence: fax 409-772-9231
Hemoglobin is composed of two
and two ß polypeptide
chains. Any modifications in the amino acid sequence, which may either
be congenital or acquired, affects the oxygen-carrying ability of
hemoglobin, resulting in a series of hemoglobinopathies. To date, >600
structurally different human hemoglobins are known
(1)(2). Identification of abnormal hemoglobin
is very important in the differential diagnosis of hemoglobinopathies.
Currently, most clinical laboratories have a battery of hemoglobin
assays that includes gel electrophoresis, ion-exchange or affinity
chromatography, and isoelectric focusing
(1)(3). Of all the available methods,
computer-operated cation-exchange HPLC is the most widely used for
identifying and quantifying major and minor hemoglobins
(4)(5)(6)(7). The main disadvantage of a HPLC system is
expensive instrumentation and the high cost of columns and reagents.
Although an excellent resolution is achieved with gel isoelectric
focusing (8), it is labor intensive, time consuming, and
not readily amenable for routine screening.
The use of capillary electrophoresis (CE) for identification of
hemoglobin variants has been reported by several authors
(9)(10)(11)(12
Footnotes
References
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