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Characterization of latex allergenic components by capillary zone electrophoresis and N-terminal sequence analysis |
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| Authors: | Hung-Dar Chen Chao-Ling Chen Shih-Wen Huang Hsiang-Fu Kung Hao-Chia Chen |
| Institution: | 1. Department of Large Animal Clinical Science, College of Veterinary Medicine, USA 2. Bldg. 567, Rm. 152, Laboratory of Biochemical Physiology Division of Basic Sciences, National Cancer Institute Frederick Cancer Research and Development Center, 21701, Frederick, MD, USA 3. Department of Veterinary Medicine, National Chung-Hsing University, Taichung, Taiwan, ROC 4. Department of Pediatrics, College of Medicine, University of Florida, Gainesville, Fla. 5. Endocrinology and Reproductive Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Md., USA |
| Abstract: | In a previous study, protein components purified from latex gloves that elicited allergenic reactions were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and yielded apparent molecular weights of 14, 22, 30, 34, 46, and 58 kD. These allergenic components were isolated for further characterization by capillary zone electrophoresis and N-terminal amino acid sequence analysis. These components all migrated at approximately 25 and 35 min on capillary zone electrophoresis. Diode array spectral analysis detected indistinguishable characteristics between these two protein peaks. In addition, complex formation of these components with patients' immunoglobulin was demonstrated by capillary zone electrophoresis. Analysis of components separated by SDS-PAGE on a polyvinylidene difluoride membrane showed that the first 13 residues were identical to the sequence of hevein. Based on the criteria of charge-to-mass ratio and N-terminall amino acid sequence, our results suggest that these components of latex proteins are similar in the primary structure. |
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