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
1989; Elsevier BV; Volume: 994; Issue: 3 Linguagem: Inglês
10.1016/0167-4838(89)90302-6
ISSN1878-1454
AutoresGundula Risse, Ursula Stochaj, Katharina Elsässer, Josef Dieckhoff, Hans Georg Mannherz, Klaus von der Mark,
Tópico(s)Protease and Inhibitor Mechanisms
ResumoThe 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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