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Characterization of latex allergenic components by capillary zone electrophoresis and N-terminal sequence analysis

  1. Author:
    Chen, H. D.
    Chen, C. L.
    Huang, S. W.
    Kung, H. F.
    Chen, H. C.

  2. Author Address

    Chen HD NCI, Frederick Canc Res & Dev Ctr, Lab Biochem Physiol, Div Basic Sci Bldg 567,Rm 152 Frederick, MD 21701 USA NCI, Frederick Canc Res & Dev Ctr, Lab Biochem Physiol, Div Basic Sci Frederick, MD 21701 USA Natl Chung Hsing Univ, Dept Vet Med Taichung 40227 Taiwan Univ Florida, Coll Vet Med, Dept Large Anim Clin Sci Gainesville, FL 32610 USA Univ Florida, Coll Med, Dept Pediat Gainesville, FL USA NICHHD, Endocrinol & Reprod Res Branch, NIH Bethesda, MD 20892 USA
    1. Year: 1998
  2. Journal: Journal of Biomedical Science
    1. 5
    2. 6
    3. Pages: 421-427
  4. Type of Article: Article
  1. 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-terminal amino acid sequence, our results suggest that these components of latex proteins are similar in the primary structure. [References: 24]

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