Abstract
Dextran T40 was oxidized with periodate to form aldehyde groups to which recombinant human growth hormone (rhGH) was attached. Complex formation involved the reversible formation of an imine conjugate and the extent of complex formation was proportional to the degree of oxidation of the dextran. The complex was characterized by a variety of techniques including SEC, SDS-PAGE and IEF. In vitro, the rate of release of rhGH from a rhGH-dextran complex was inversely proportional to the degree of oxidation of the dextran. The released protein was characterized by peptide mapping, N-terminal sequencing, SEC and SDS-PAGE. Sustained release of rhGH was observed in vivo, based on the observation of significant weight gain in a rat bioassay.
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