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
- 8Citations
- 3Captures
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Metrics Details
- Citations8
- Citation Indexes8
- CrossRef3
- Captures3
- Readers3
Article Description
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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0167483889903026; http://dx.doi.org/10.1016/0167-4838(89)90302-6; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0024495107&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/2465783; https://linkinghub.elsevier.com/retrieve/pii/0167483889903026; http://dx.doi.org/10.1016/0167-4838%2889%2990302-6; https://dx.doi.org/10.1016/0167-4838%2889%2990302-6
Elsevier BV
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