Presence of Immunologically Active Fragments after Proteolytic Degradation of Human γ-Globulin

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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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  1. 1

    Lapresle, C., Kaminski, M., and Tanner, C. E., J. Immunol., 82, 94 (1959).

  2. 2

    Lapresle, C., Webb, T., Kaminski, M., and Champagne, M., Bull. Soc. Chim. Biol., 41, 695 (1959).

  3. 3

    Porter, R. R., Biochem. J., 66, 677 (1957).

  4. 4

    Porter, R. R., Nature, 182, 670 (1958).

  5. 5

    Gorini, L., and Felix, F., Biochim. Biophys. Acta, 11, 535 (1953).

  6. 6

    Grabar, P., and Williams, C. A., Biochim. Biophys. Acta, 17, 67 (1955).

  7. 7

    Porath, J., and Flodin, P., Nature, 183, 1657 (1959).

  8. 8

    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) doi:10.1038/187599a0

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