Abstract
An enzyme immunoassay of bradykinin was developed by using ß-D-galactosidase as a labeling enzyme. Bradykinin was conjugated to ß-D-galactosidase with a new coupling agent of a hetero bis-functional type, N-(m-maleimidobenzoyloxy)-succinimide (MBS). Antisera were obtained from rabbits immunized with bradykinin linked to albumins (ovalbumin or bovine serum albumin) with toluene2,4-diisocyanate. Double antibody method was employed to separate the antibody-bound antigen from free. The enzyme activity in the precipitate was measured with a fluorogenic substrate, 4-methyl umbelliferyl-ß-D-galactoside. This assay is based on heterogeneous competitive binding between unlabeled and labeled antigens, so that unlabeled bradykinin reduces binding of bradykinin-enzyme conjugates to the antibody. A standard inhibition curve was linear between 3 and 300 ng bradykinin/assay tube.
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Ueno, A., Oh-Ishi, S., Kitagawa, T., Katori, M. (1979). Enzyme Immunoassay of Bradykinin. In: Fujii, S., Moriya, H., Suzuki, T. (eds) Kinins—II. Advances in Experimental Medicine and Biology, vol 120. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-0926-1_19
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DOI: https://doi.org/10.1007/978-1-4757-0926-1_19
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