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THE USE OF HOMOCARNOSINE AS A SPACER IN INDIRECT HAEMAGGLUTINATION
Author(s) -
Dalen Are B.
Publication year - 1977
Publication title -
acta pathologica microbiologica scandinavica section c immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0304-1328
DOI - 10.1111/j.1699-0463.1977.tb03640.x
Subject(s) - chemistry , histidine , lability , glutaraldehyde , reagent , hemagglutination , tyrosine , medicinal chemistry , polymer chemistry , biochemistry , antibody , chromatography , organic chemistry , amino acid , immunology , biology
Homocarnosine (γ‐butyryl‐L‐histidine) was bound to erythrocytes through the action of glutaraldehyde in order to increase the number of available groups for diazotization on the surface of the cells. Diazotization was performed with tetrazotizized di‐o‐anisidine (TOD). TOD decomposed rapidly at an alkaline pH. The reagent was stabilized by the use of borate buffers. The presence of homocarnosine on erythrocytes enhanced the coupling of histidine by diazotization. TOD formed bonds of varying lability with alifatic amino and imino groups. This inhibited completely the formation of stable bonds with histidine and tyrosine. The relative amounts of stable bonds formed by TOD and human serum albumin and TOD and γ‐globulin varied inversely with the concentration of the proteins. The two proteins were used as model antigens and the presence of homocarnosine on the surface of the erythrocytes increased the sensitivity of the haemagglutination reaction by a factor of 4–8.