On the agglutinogens of red cells developed with proteolytic enzymes and neuraminidase.
It has been known that the agglutinability of human red cells is changed or enhanced by treatments with proteolytic enzymes or neuraminidase. In this paper, the serological properties of agglutinogens developed by proteolytic enzymes (bromelin, ficin, papain, trypsin and pronase) and neuraminidase are investigated by using antisera to trypsin- and neuraminidase-treated red cells. The adsorptions of the antiserum to trypsinized red cells with the cells treated with each of the proteolytic enzymes showed that the agglutinogens uncovered by bromelin, ficin and papain were different from those by pronase and trypsin. It was demonstrated that pronase was the most effective enzyme to uncover the agglutinogen located on deeper site of red cell membrane. This was confirmed by the agglutination with the test cells treated twice with two kinds of the enzymes. The reactions of the antiserum to neuraminidase-treated red cells treated with six kinds of the enzymes indicated that the agglutinogens developed by neuraminidase resembled those by bromelin, ficin and papain more than those by trypsin and pronase.
D000373:Agglutinins / Q000378:metabolism*; D004912:Erythrocytes / Q000187:drug effects* / Q000378:metabolism; D006384:Hemagglutination / Q000187:drug effects; D006388:Hemagglutinins / Q000378:metabolism*; D006801:Humans; D007106:Immune Sera; D008951:MNSs Blood-Group System; D009439:Neuraminidase / Q000276:immunology / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000494:pharmacology*; D011498:Protein Precursors / Q000378:metabolism*; D014357:Trypsin / Q000276:immunology / Q000494:pharmacology
D000373:Agglutinins; D006388:Hemagglutinins; D007106:Immune Sera; D008951:MNSs Blood-Group System; D011498:Protein Precursors; D009439:Neuraminidase; D010447:Peptide Hydrolases; D014357:Trypsin