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J. Biochem, 1981, Vol. 89, No. 4 1091-1099
© 1981 Japanese Biochemical Society

research-article

Highly Specific Enzyme Immunoassay for Human Chorionic Gonadotropin

Susumu IWASA, Chieko KITADA, Isamu YOSHIDA, Koichi KONDO, Masatake HORI and Masahiko FUJINO

Chemical Research Laboratories, Central Research Division, Takeda Chemical Industries, Ltd. Jusohonmachi, Yodogawa-ku, Osaka, Osaka 532

A highly specific enzyme immunoassay for determining hCG was established by using ß-D-galactosidase as label. In order to increase the specificity of the assay, an antiserum against whole hCG was purified on a column of hCGß carboxyl-terminal peptide (residues 123–145) covalently linked to Sepharose 4B. The antibody (N101S) thus prepared showed a weak cross-reactivity with human LH in an assay using hCG-enzyme conjugate, but the slight cross-reactivity was virtually avoided when an hCG0 carboxyl-terminal peptide was used as a peptide in the enzyme conjugate.

N101S antibody was compared with antiserum (BIB) directed against a carboxyl-terminal peptide (123–145). In hCG measurement N101S gave about 30 times higher sensitivity than BIB, although the former antibody was less sensitive to carboxyl-terminal peptides of hCGß. The enzyme immunoassay using a combination of N101S antibody and a carboxyl-terminal peptide (130–145)-enzyme conjugate was able to detect as little as 0.25 mlU of hCG without the interference of LH. The performance and validity of this assay were comparable to those of conventional radioimmunoassay.


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