Abstract
ACCORDING to Lapresle, Kaminski and Tanner1, degradation of human serum albumin with trypsin or chymotrypsin yields several components with retained ability to give precipitation reactions with anti-human albumin antibodies. One of these components has been isolated by column electrophoresis in an agar medium and partially characterized by ultracentrifugation2. Porter3 isolated and characterized a similar component after chymotryptic hydrolysis of bovine serum albumin. After degradation of rabbit γ-globulin with papain, Porter also isolated a component showing inhibitory properties when added to a rabbit γ-globulin–anti-γ-globulin system4.
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References
Lapresle, C., Kaminski, M., and Tanner, C. E., J. Immunol., 82, 94 (1959).
Lapresle, C., Webb, T., Kaminski, M., and Champagne, M., Bull. Soc. Chim. Biol., 41, 695 (1959).
Porter, R. R., Biochem. J., 66, 677 (1957).
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Gorini, L., and Felix, F., Biochim. Biophys. Acta, 11, 535 (1953).
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Porath, J., and Flodin, P., Nature, 183, 1657 (1959).
Scheidegger, J.-J., and Buzzi, C., Rev. franc. Et. clin. biol., 2, 895 (1957).
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HANSON, L., JOHANSSON, B. Presence of Immunologically Active Fragments after Proteolytic Degradation of Human γ-Globulin. Nature 187, 599–600 (1960). https://doi.org/10.1038/187599a0
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DOI: https://doi.org/10.1038/187599a0
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