Abstract
1. 1. The sialic acid residues of human α 1-protease inhibitor were modified by periodate oxidation and subsequent reductive amination with ethanolamine and sodium cyanoborohydride. 2. 2. The modified inhibitor retained its original trypsin inhibitory activity and was not digested by neuraminidase from Clostridium perfringens. 3. 3. The modified inhibitor disappeared from rat blood circulation at the same rate as the native inhibitor.
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