Preparation of neuraminidase-resistant human alpha 1-protease inhibitor and its clearance in rat blood circulation.
The sialic acid residues of human alpha 1-protease inhibitor were modified by periodate oxidation and subsequent reductive amination with ethanolamine and sodium cyanoborohydride. The modified inhibitor retained its original trypsin inhibitory activity and was not digested by neuraminidase from Clostridium perfringens. The modified inhibitor disappeared from rat blood circulation at the same rate as the native inhibitor.
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D001894:Borohydrides; D055598:Chemical Phenomena; D002621:Chemistry; D019856:Ethanolamine; D004983:Ethanolamines; D006801:Humans; D008657:Metabolic Clearance Rate; D009439:Neuraminidase / Q000494:pharmacology*; D010084:Oxidation-Reduction; D010504:Periodic Acid; D051381:Rats; D012794:Sialic Acids; D013329:Structure-Activity Relationship; D000515:alpha 1-Antitrypsin
D001798:Blood Proteins; D001894:Borohydrides; D004983:Ethanolamines; D012794:Sialic Acids; D000515:alpha 1-Antitrypsin; D010504:Periodic Acid; D019856:Ethanolamine; C009282:sodium cyanoborohydride; D009439:Neuraminidase