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Hydrophobic chromatography of fibronectin
Author(s) -
Morgenthaler J.-J.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81308-2
Subject(s) - fibronectin , chemistry , gelatin , hydrophobic effect , elution , chromatography , methylene , hydrophilic interaction chromatography , polymer chemistry , organic chemistry , biochemistry , extracellular matrix , high performance liquid chromatography
Fibronectin was chromatographed on immobilized alkanes of various chain lengths. No binding of the protein to the hydrophobic matrix was observed with alkanes containing from 3–7 methylene groups; the protein bound, however, to immobilized alkanes with 8 or 10 methylene groups. Fibronectin could be quantitatively eluted from commercial Octylsepharose with a non‐ionic detergent. A gelatin‐based plasma expander did not interfere with the binding. Many proteolytic fibronectin fragments also bound to a hydrophobic matix. The results show that fibronectin posesses at least one hydrophobic binding site.