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Abstract
The relationship between soluble and insoluble proteins in the bovine, human and dogfish lens has been studied by immuno-electrophoresis and urea starch gel electrophoresis at pH 3.0. The result from the immuno-electrophoresis experiment indicated that insoluble protein derived from bovine and human lens is composed of <i>α</i>- and <i>β</i>-crystallins while that obtained from dogfish lens contains <i>γ</i>- and <i>β</i>-crystallins. The urea starch gel electrophoretic patterns of <i>α</i>-crystallin and insouble protein in bovine and human lens showed considerable similarity, however, those of dogfish <i>γ</i>-crystallin and dogfish insoluble protein showed significant differences in their mobilities. The cross-reaction between bovine <i>α</i>-crystallin and bovine insoluble suspension was studied by the quantitative complement fixation test, using rabbit antisera to bovine <i>α</i>-crystallin. The results indicated that 5 to 10% of the total insoluble protein has <i>α</i>-crystallin in a form available for the reaction with the antibody. Similar results were observed when dogfish <i>γ</i>-crystalin and dogfish insoluble suspension was studied.
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