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Characterization of an Antiserum against Feather Keratins of the Chick: Its Crossreaction with a Lens Protein, δ‐crystallin
Author(s) -
KODAMA RYUJI,
EGUCHI GORO
Publication year - 1983
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.1983.00261.x
Subject(s) - antiserum , antigenicity , keratin , ouchterlony double immunodiffusion , feather , immunodiffusion , crystallin , staining , precipitin , microbiology and biotechnology , chemistry , polyacrylamide gel electrophoresis , lens (geology) , gel electrophoresis , solubilization , biology , biochemistry , antibody , enzyme , immunology , ecology , genetics , paleontology
We prepared an antiserum against a fraction of solubilized keratins extracted from down feathers of newly hatched chicks. The specificity of the antiserum was tested by double immunodiffusion, immunofluorescent staining, and immunoblotting after sodium dodecylsulfate‐polyacrylamide gel electrophoresis. All the bands except “Fast protein” reacted with the antiserum, suggesting the presence of a common antigenicity through various polypeptides in solubilized feather keratins. Delta‐crystallin, which is a lens specific protein, also reacted with the antiserum. The presence of a common antigenicity between δ‐crystallin and feather and scale keratins was confirmed by affinity‐purification of the antiserum, and its significance is discussed.