Effect of Proteolytic Digestion on the Structure and Function of Human Properdin

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Abstract
Human properdin P̄ was found to be sensitive to the action of trypsin, chymotrypsin, pepsin, and Streptomycetes caesipitosus protease. Incubation of P̄ with these enzymes resulted in loss of tis founctional activity and the productin of antigenically deficient components compared to untreated P̄. Upon incubation with trypsin, P̄ was initially cleaved into a minor fragment and a major fragment. Further degradation of the fragments occurred with prolongation of inculation time.The minor fragment wa highly susceptible to further proteolysis compared to the major fragment which contained fthe carbohydrate moiety of the molecule. SDS-polyacrylamide gel electrophoretic analysis of trypsin-digested P̄ suggested that the subunit polypeptide chains were initially cleaved at similar points to produce the major and minor fragments. The sedimentation velocity of the major fragment was higher than that of the intact molecule. The implications of these observations of the configuration of P̄ are discussed.

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