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Separation of components of human globulins by capillary zone electrophoresis using a linear polyacrylamide-coated capillary
Eleven commercially available protein preparations from human serum were subjected to capillary zone electrophoresis (CZE) using a linear polyacrylamide-coated capillary at pH 7.4. Transferrin, complement C3 and C-reactive protein were each separated into one major peak and several minor peaks. α 1-...
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Published in: | Journal of chromatography. B, Biomedical sciences and applications Biomedical sciences and applications, 1997-09, Vol.697 (1), p.217-222 |
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Main Author: | |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Eleven commercially available protein preparations from human serum were subjected to capillary zone electrophoresis (CZE) using a linear polyacrylamide-coated capillary at pH 7.4. Transferrin, complement C3 and C-reactive protein were each separated into one major peak and several minor peaks.
α
1-Antitrypsin was separated into two major peaks and three minor peaks.
α
2-HS-glycoprotein showed four major peaks with a leading shoulder. Haptoglobin,
α
2-microglobulin,
α
1-acid-glycoprotein and prealbumin were detected as relatively wide peaks. Ceruloplasmin showed one major peak with notches, and two minor and several notched peaks. Only low density lipoprotein showed no peaks. A mixture of five of the protein preparations was separated into individual components, as well as individual isoforms. When the same mixture was analyzed by CZE using an uncoated capillary, a much poorer resolution was obtained. Application of this CZE system to albumin-depleted serum demonstrated that it is very useful for analyzing globulin components in serum. |
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ISSN: | 0378-4347 1387-2273 |
DOI: | 10.1016/S0378-4347(97)00131-X |