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Structural comparison of the 68 kDa laminin-binding protein and 5′-nucleotidase from chicken muscular sources: Evidence against a gross structural similarity of both proteins

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, ISSN: 0167-4838, Vol: 994, Issue: 3, Page: 258-263
1989
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The 68 kDa laminin-binding protein purified from chicken skeletal muscle and the ectoenzyme 5′-nucleotidase from chicken gizzard are both able to interact with laminin. They were both shown to possess a nearly identical amino acid composition. The 79 kDa glycosylated form of 5′-nucleotidase can be transformed into an enzymatically active form by treatment with endoglycosidase F (Endo F). Deglycosylated (Endo F-treated) 5′-nucleotidase exhibits an apparent molecular mass of 68 kDa. Using immunological and finger-printing techniques, both proteins were analysed to determine their structural relatedness. The results obtained indicate that both proteins are not identical but may possess a few common peptides of yet unknown sequence and length.

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