Polyvinylpyrrolidone (PVP) oligomers with -OH terminal groups, obtained by radical polymerization using 2-mercaptoethanol as chain-transfer agent, were fractionated by gel chromatography to obtain a product with an approximate molecular weight of 1100. The hydroxyl function of such oligomer was activated with 4-nitrophenyl chloroformate to give an active carbonate derivative suitable for linking to peptide or protein amino groups in aqueous media buffered at mild alkaline pH. The linking of the PVP to the protein surface was accomplished without loss of enzymatic activity in the model enzyme ribonuclease. When the polymerization of PVP is carried out using 2-mercaptoacetic acid as chain-transfer agent, a much more heterogeneous product was obtained. Also this, activated as succinimidyl ester, could also be bound to amine groups; however, this treatment performed on the model enzyme RNase caused inactivation.
Hydroxyl-terminated poly(vinylpyrrolidone) for the modification of polypeptides / V. M. F, S. L., C. P., S. O., E. Ranucci, F. P.. - In: JOURNAL OF BIOACTIVE AND COMPATIBLE POLYMERS. - ISSN 0883-9115. - 5:2(1990), pp. 167-178.
|Titolo:||Hydroxyl-terminated poly(vinylpyrrolidone) for the modification of polypeptides|
|Settore Scientifico Disciplinare:||Settore CHIM/04 - Chimica Industriale|
|Data di pubblicazione:||1990|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1177/088391159000500202|
|Appare nelle tipologie:||01 - Articolo su periodico|