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J. Biochem, 1970, Vol. 67, No. 2 313-323
© 1970 Japanese Biochemical Society

research-article

Studies on the Structure of Bovine Kininogen: Cleavages of Disulfide Bonds and of Methionyl Bonds in Kininogen-II

HISAO KATO, SHIGEHARU NAGASAWA and TOMOJI SUZUKI

Division of Plasma Proteins, Institute for Protein Research, Osaka University Osaka

The possible numbers of sulfhydryl groups and disulfide bridges in bovine kininogen-II*, which is a precursor protein of physiologically active peptide, bradykinin or kallidin, have been evaluated by means of 14C-monoiodoacetic acid before or after the reduction with ß-mercaptoethanol and by means of amino acid analysis after reduction and alkylation. The figures were in good agreement and no sulfhydryl groups were detectable even in the presence of 8 M urea, and suggest that all half cystine residues participate in the formation of disulfide bridges. Approximately seven disulfide bonds were determined per molecule, assuming a molecular weight of about 50, 000.

Immunological properties of intact kininogen-II and its modified proteins were examined with antikininogen-II antibody prepared from immunized rabbit serum. In immunoelectrophoresis, two precipitin lines of the kininogen-II against the antibody were observed, suggesting tendency with an antigenic heterogeneity or microheterogeneity of the intact protein. On immunodiffusion, both native and kinin-free-kininogen reacted identically with the antikininogen antibody. However, no cross-reaction was found between the S-carboxymethylated protein and the antibody, indicating complete abolishment of the antigenic activity by the destruction of disulfide bonds. Kinin-free-kininogen cross-reacted positively with the antikininogen antibody and this suggests that the kinin moiety in the polypeptide chain of kininogen cross-reacted positively with the antikininogen antibody and this suggests that the kinin moiety in the polypeptide chain of kininogen molecule does not participate in formation of the antibody as a determinant group.

Treatment of bovine kininogen-II with cyanogen bromide produced a fragment containing kinin peptide sequence. The BrCN-fragment was deduced to have following amino acid sequence:

Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Val-Gln-Val-Homoser


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