Zobrazeno 1 - 3
of 3
pro vyhledávání: '"J. C. Pinder"'
Publikováno v:
European Biophysics Journal. 28:208-215
We have examined the properties and interactions of expressed polypeptide fragments from the N-terminus of the alpha-chain and the C-terminus of the beta-chain of human erythroid spectrin. Each polypeptide comprises one complete structural repeating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f36efaeb9a067c673f43800246002d9a
https://doi.org/10.1007/s002490050201
https://doi.org/10.1007/s002490050201
Publikováno v:
Blood. 82(11)
The identity of the membrane binding sites for the membrane cytoskeletal protein 4.1 of the human red blood cell has been investigated. Exhaustive proteolysis of the membrane with a range of proteases led to the elimination of only some 60% of all bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::58a66ef24ead5918f86ee55fc82be68b
https://pubmed.ncbi.nlm.nih.gov/8068957
https://pubmed.ncbi.nlm.nih.gov/8068957
Autor:
G H, Beaven, L, Jean-Baptiste, E, Ungewickell, A J, Baines, F, Shahbakhti, J C, Pinder, S E, Lux, W B, Gratzer
Publikováno v:
European journal of cell biology. 36(2)
A part of the spectrin extracted from red cell membranes at low ionic strength occurs in the form of a high-molecular weight oligomeric complex with actin and proteins 4.1 and 4.9. When the extraction is performed at 35 degrees, the spectrin is prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3fcf22c0a64eaa2dfdef64c7e7476a52
https://pubmed.ncbi.nlm.nih.gov/4039666
https://pubmed.ncbi.nlm.nih.gov/4039666