Abstract
Analyses by SDS-polyacrylamide gel electrophoresis of plasma membranes isolated from a rebion of the chick lens (outer cortex) where little or no (<1.0%) soluble δ-crystalline is present confirmed the presence of δ-crystallin in the membranes, ruling out the possibility that this component constitutes a contaminant in the membranes of soluble fraction origin. Delta-crystalline (polypeptide 11) comprised 38% of the protein recovered in the membrane fraction of the chick lens outer cortex. Immunological reactions utilizing an antiserum prepared in rabbits against the isolated membrane component confirmed its identity as δ-crystallin. Several (2–3) immunologically identical δ-crystalline subunits, ranging in molecular weight from 43 000 to 48 000 D, were consistently observed to be present in membranes from the 17-day embryonic and adult cortical lens fiber cells; only the 43 000 molecular weight subunit appeared to be present in the membranes of the adult lens nucleus. The exact role of membrane crystallins in lens fiber cell differentiation now remains open to further investigation.
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