An enzyme immunoassay for K-76 monocarboxylic acid, a novel anticomplementary compound.
A competitive enzyme immunoassay for K-76 monocarboxylic acid (K-76COOH), a novel anticomplementary compound, was developed. K-76COOH was directly coupled with bovine serum albumin through a formation of Schiff base and successive reduction. The spectral data of the conjugate showed no evidence of a Schiff base form. Using the specific antiserum, the proposed homologous assay made it possible to detect K-76COOH at the lowest value of 1 ng/ml of plasma. The immunoassay was validated by the correlation with HPLC analyses. The time courses of plasma levels of K-76COOH after a single oral administration to beagle dogs were precisely determined with a very low absorption efficiency. From these results, it is suggested that the plasma values obtained are insufficient for K-76COOH to exert its anticomplementary action in vivo; thus K-76COOH may have another immunopharmacological function.
Yamamoto
I
I
Department of Immunochemistry, Faculty of Pharmaceutical Sciences, Okayama University, Japan.
Muto
N
N
Murakami
K
K
Suga
S
S
D000818:Animals; D000917:Antibody Formation; D000918:Antibody Specificity; D003429:Cross Reactions; D004285:Dogs; D004797:Enzyme-Linked Immunosorbent Assay; D007124:Immunoenzyme Techniques; D015394:Molecular Structure; D051381:Rats; D012545:Schiff Bases / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000378:metabolism; D012717:Sesquiterpenes / Q000097:blood* / Q000633:toxicity*; D013997:Time Factors
D012545:Schiff Bases; D012717:Sesquiterpenes; D012710:Serum Albumin, Bovine; C038797:K 76 carboxylic acid