Detection of eosinophil cationic protein (ECP) by an enzyme-linked immunosorbent assay

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Detection of eosinophil cationic protein (ECP) by an enzyme-linked immunosorbent assay. / Reimert, C M; Venge, P; Kharazmi, A; Bendtzen, K.

In: Journal of Immunological Methods, Vol. 138, No. 2, 1991, p. 285-90.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Reimert, CM, Venge, P, Kharazmi, A & Bendtzen, K 1991, 'Detection of eosinophil cationic protein (ECP) by an enzyme-linked immunosorbent assay', Journal of Immunological Methods, vol. 138, no. 2, pp. 285-90.

APA

Reimert, C. M., Venge, P., Kharazmi, A., & Bendtzen, K. (1991). Detection of eosinophil cationic protein (ECP) by an enzyme-linked immunosorbent assay. Journal of Immunological Methods, 138(2), 285-90.

Vancouver

Reimert CM, Venge P, Kharazmi A, Bendtzen K. Detection of eosinophil cationic protein (ECP) by an enzyme-linked immunosorbent assay. Journal of Immunological Methods. 1991;138(2):285-90.

Author

Reimert, C M ; Venge, P ; Kharazmi, A ; Bendtzen, K. / Detection of eosinophil cationic protein (ECP) by an enzyme-linked immunosorbent assay. In: Journal of Immunological Methods. 1991 ; Vol. 138, No. 2. pp. 285-90.

Bibtex

@article{7e29d060207b11df8ed1000ea68e967b,
title = "Detection of eosinophil cationic protein (ECP) by an enzyme-linked immunosorbent assay",
abstract = "Eosinophil cationic protein (ECP) is a highly basic and potent cytotoxic single-chain zinc-containing protein present in the granules of the eosinophilic granulocytes. ECP appears to be involved in defence against parasites and in the tissue damage seen in subjects with allergic and inflammatory disease. To investigate ECP release from in vitro activated human eosinophils and to study the involvement of eosinophils in health and disease, we have developed a sensitive and specific enzyme immunoassay. ECP was purified from normal human peripheral blood eosinophils and polyclonal antibodies to ECP were subsequently raised in rabbits. The ELISA utilizes the biotin/avidin method and measures ECP within the range 15-1000 ng/l. The intra- and interassay coefficients of variation were 6% and 10%, respectively, and the recoveries of 12 and 25 pg of purified ECP added to diluted serum samples were 108 +/- 14.5% (mean +/- SD, n = 12) and 107 +/- 7.5%, respectively. The high sensitivity, reproducibility and specificity of this ELISA makes it suitable for the determination of minute amounts of ECP in in vitro systems as well as in various biological fluids.",
author = "Reimert, {C M} and P Venge and A Kharazmi and K Bendtzen",
note = "Keywords: Blood Proteins; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Eosinophil Granule Proteins; Eosinophils; Humans; Immunoelectrophoresis; Lymphocyte Activation; Radioimmunoassay; Reproducibility of Results; Ribonucleases; Sensitivity and Specificity",
year = "1991",
language = "English",
volume = "138",
pages = "285--90",
journal = "Journal of Immunological Methods",
issn = "0022-1759",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Detection of eosinophil cationic protein (ECP) by an enzyme-linked immunosorbent assay

AU - Reimert, C M

AU - Venge, P

AU - Kharazmi, A

AU - Bendtzen, K

N1 - Keywords: Blood Proteins; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Eosinophil Granule Proteins; Eosinophils; Humans; Immunoelectrophoresis; Lymphocyte Activation; Radioimmunoassay; Reproducibility of Results; Ribonucleases; Sensitivity and Specificity

PY - 1991

Y1 - 1991

N2 - Eosinophil cationic protein (ECP) is a highly basic and potent cytotoxic single-chain zinc-containing protein present in the granules of the eosinophilic granulocytes. ECP appears to be involved in defence against parasites and in the tissue damage seen in subjects with allergic and inflammatory disease. To investigate ECP release from in vitro activated human eosinophils and to study the involvement of eosinophils in health and disease, we have developed a sensitive and specific enzyme immunoassay. ECP was purified from normal human peripheral blood eosinophils and polyclonal antibodies to ECP were subsequently raised in rabbits. The ELISA utilizes the biotin/avidin method and measures ECP within the range 15-1000 ng/l. The intra- and interassay coefficients of variation were 6% and 10%, respectively, and the recoveries of 12 and 25 pg of purified ECP added to diluted serum samples were 108 +/- 14.5% (mean +/- SD, n = 12) and 107 +/- 7.5%, respectively. The high sensitivity, reproducibility and specificity of this ELISA makes it suitable for the determination of minute amounts of ECP in in vitro systems as well as in various biological fluids.

AB - Eosinophil cationic protein (ECP) is a highly basic and potent cytotoxic single-chain zinc-containing protein present in the granules of the eosinophilic granulocytes. ECP appears to be involved in defence against parasites and in the tissue damage seen in subjects with allergic and inflammatory disease. To investigate ECP release from in vitro activated human eosinophils and to study the involvement of eosinophils in health and disease, we have developed a sensitive and specific enzyme immunoassay. ECP was purified from normal human peripheral blood eosinophils and polyclonal antibodies to ECP were subsequently raised in rabbits. The ELISA utilizes the biotin/avidin method and measures ECP within the range 15-1000 ng/l. The intra- and interassay coefficients of variation were 6% and 10%, respectively, and the recoveries of 12 and 25 pg of purified ECP added to diluted serum samples were 108 +/- 14.5% (mean +/- SD, n = 12) and 107 +/- 7.5%, respectively. The high sensitivity, reproducibility and specificity of this ELISA makes it suitable for the determination of minute amounts of ECP in in vitro systems as well as in various biological fluids.

M3 - Journal article

C2 - 2033280

VL - 138

SP - 285

EP - 290

JO - Journal of Immunological Methods

JF - Journal of Immunological Methods

SN - 0022-1759

IS - 2

ER -

ID: 18177914