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Coupling of poly(ethylene glycol) to albumin under very mild conditions by activation with tresyl chloride: characterization of the conjugate by partitioning in aqueous two‐phase systems
Author(s) -
Delgado C.,
Patel JN,
Francis GE,
Fisher D.
Publication year - 1990
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1990.tb00085.x
Subject(s) - ethylene glycol , aqueous solution , partition coefficient , chemistry , chloride , conjugate , albumin , polymer chemistry , serum albumin , ethylene , chromatography , nuclear chemistry , organic chemistry , biochemistry , catalysis , mathematical analysis , mathematics
Poly(ethylene glycol) activated with tresyl chloride has been covalently linked to albumin as a result of a 2‐h incubation in 0.05 M sodium phosphate buffer, pH 7.5, containing 0.125 M sodium chloride (0.344 OSM). The coupling of poly(ethylene glycol) to albumin was demonstrated by the increase in the partition coefficient of the protein in poly(ethylene glycol)‐dextran aqueous two‐phase systems. A linear relationship between the log of the partition coefficient of the poly(ethylene glycol)‐albumin conjugate and the degree of modification (measured as the amino groups consumed during the coupling step) has been demonstrated. Countercurrent distribution in the two‐phase system showed that poly(ethylene glycol)‐albumin was heterogeneous with respect to its partitioning behavior, indicating that the albumin was not uniformly modified with poly(ethylene glycol).