
doi: 10.1002/jcb.10574
pmid: 12874826
AbstractParalemmin was identified in the chicken lens as a protein with mol. wt 65 kDa and a splice variant of 60 kDa, both soluble in Triton X‐100. Paralemmin is localized to the plasma membrane of fiber cells, and was not detected in the annular pad cells. Thus in the chick lens it is another feature of fiber cell differentiation. Its localization to the short side of the fiber cell and the sites of fiber cell interlocking suggests that paralemmin may play a role in the development of such interdigitating processes. J. Cell. Biochem. 89: 917–921, 2003. © 2003 Wiley‐Liss, Inc.
Cell Membrane, Immunoblotting, Molecular Sequence Data, Fluorescent Antibody Technique, Membrane Proteins, Cell Differentiation, Epithelial Cells, Phosphoproteins, Peptide Fragments, Molecular Weight, Lens, Crystalline, Animals, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Chickens
Cell Membrane, Immunoblotting, Molecular Sequence Data, Fluorescent Antibody Technique, Membrane Proteins, Cell Differentiation, Epithelial Cells, Phosphoproteins, Peptide Fragments, Molecular Weight, Lens, Crystalline, Animals, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Chickens
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