Purificaiton and characterization of mouse serum protein with specific binding affinity for C4 (Ss protein).
A new component of the complement (C).system, with a specific binding affinity for the activated Ss-protein (C4) has been identified in mouse serum. This protein, named Ss- (or C4)-binding protein (Ss-bp), was purified about 200 times from mouse plasma. Ss-bp is a heat stable (56 degrees C, 60 rain) beta-globulin with a sedimentation coefficient in sucrose density ultracentrifugation of 10s. Its concentration in serum of adult male and female mice is 160 and 60 mug/ml, respectively. In EDTA-plasma, Ss and Ss-bp are not associated and can be separated by chromatography in Sephadex G-200. However, in serum Ss-bp binds tightly to Ss. The bonds between these proteins cannot be reversed by chelation of divalent cations. As a consequence of the formation of Ss/Ss-bp complexes, the properties of Ss-bp appear to be quite different in serum of mice with high (Ss-H) or low (Ss-L) levels of Ss-protein. In Ss-H serum, all of Ss- bp is bound to Ss. In Ss-L serum, Ss-bp is mostly free. Because the electrophoretic mobilities of free and complexed Ss-bp are quite different, Ss-bp appears to be polymorphic in serum (but not in EDTA- plasma). The strict dependency of the apparent electrophoretic mobility of Ss-bp on the levels of Ss in serum was demonstrated in a series of congenic mice and among the progeny of a cross between Ss-H and Ss-L strains of mice. Without exception, the slow and fast varieties of Ss-bp were associated with the Ss-L and Ss-H traits. Ss-bp of the slow variety can be transformed into the fast variety by addition of pure human C4, or C4-sufficient guinea pig serum, to Ss-L serum. In both instances Ss-bp formed stable complexes with C4 or a C4- derived peptide. These findings highlight the binding specificity of Ss- bp for the fourth component of the complement system, and in addition they demonstrate a functional homology between the Ss-protein and C4 from two different species.
D000818:Animals; D001798:Blood Proteins / Q000302:isolation & purification* / Q000378:metabolism; D003181:Complement C4 / Q000378:metabolism*; D003165:Complement System Proteins / Q000378:metabolism*; D005260:Female; D005796:Genes; D008040:Genetic Linkage; D006168:Guinea Pigs; D006649:Histocompatibility Antigens; D006801:Humans; D008297:Male; D051379:Mice; D008970:Molecular Weight; D011485:Protein Binding; D012737:Sex Factors; D013045:Species Specificity
D001798:Blood Proteins; D003181:Complement C4; D006649:Histocompatibility Antigens; D003165:Complement System Proteins