May 1992
Volume 33, Issue 6
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Articles  |   May 1992
Identification of a major continuous epitope of human alpha crystallin.
Author Affiliations
  • L Takemoto
    Division of Biology, Kansas State University, Manhattan 66506.
  • T Emmons
    Division of Biology, Kansas State University, Manhattan 66506.
Investigative Ophthalmology & Visual Science May 1992, Vol.33, 2024-2028. doi:
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      L Takemoto, T Emmons; Identification of a major continuous epitope of human alpha crystallin.. Invest. Ophthalmol. Vis. Sci. 1992;33(6):2024-2028.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Human lens proteins were digested with trypsin or V8 protease, and the resulting peptides resolved on a C18 reverse phase column. Fractions from this column were probed with polyclonal antiserum made against the whole alpha crystallin molecule. Peptides in the seropositive fraction were purified to homogeneity, then characterized by mass spectral analysis and partial Edman degradation. The tryptic and V8 digests contained only one seropositive peptide that was derived from the C-terminal region of the alpha-A molecule. To determine the exact boundaries of the epitope, various size analogues of this region were synthesized and probed with anti-alpha serum. Together, these studies demonstrate that the major continuous epitope of the alpha-A chain includes the sequence KPTSAPS, corresponding to residues 166-172 of the human alpha-A crystallin chain.

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