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- Kärkkäinen, T, et al.
(författare)
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Isolation and immunologic properties of a heterogeneous antigen with the characteristics of the heavy chain of human plasma kininogen
- 1982
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Ingår i: Molecular Immunology. - : Elsevier BV. - 0161-5890 .- 1872-9142. ; 19:1, s. 179-189
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Tidskriftsartikel (refereegranskat)abstract
- Kininogen antigen was purified from human plasma fraction IV by ion exchange chromatography, gel filtration and affinity chromatography with antibody specific immunoadsorbents. The immunologically pure glycoprotein had a mol. wt of approximately 60,000 and only one polypeptide chain by SDS-PAGE. An extensive charge heterogeneity by isoelectric focusing and gel filtration on polyacrylamide agarose could only in part depend on a comparatively high sialic acid content, but may be caused by differences in the carbohydrate structures sustained by lectin-binding heterogeneity on Con A-Sepharose. This antigen shares a dominating determinant with native plasma kininogens shown by complete patterns of identity in immunochemical analyses and with the monospecific antisera developed in rabbits against the heterogeneous components. The similar size, amino acid composition, low histidine content, lack of N-terminal amino acid and antigenic homogeneity fit all the so far known characteristics of the human kininogen heavy chain. Notably the antigenic determinant is resistant to degradation by activated kallikrein. This antigen with unimpaired immunologic activity may be a useful tool for preparation of antiserum for immunochemical determination of human plasma kininogen.
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| 2. |
- Ragnarsson, U, et al.
(författare)
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Potentiation of bradykinin with synthetic peptides on guinea pig ileum
- 1981
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Ingår i: International journal of peptide and protein research. - 0367-8377. ; 18:1, s. 61-68
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Tidskriftsartikel (refereegranskat)abstract
- Potentiation of the activity of bradykinin on the isolated guinea pig ileum was studied using a designed test system with the synthetic peptides Leu-Val-Glu-Ser-Ser-Lys, Thr-Pro-Val-Ser-Glu-Lys, derivatives of the former coupled to the N- and C-terminals of bradykinin and two peptides with phenylalanine substituted with its isomer L-3-amino-3-phenylpropanoic acid in the 5- and 5,8-positions in bradykinin respectively. On average, two times potentiation effects were obtained at 10-6 to 10-8 M concentrations of the peptides. After elimination of the basic lysine no potentiation occurred with synthetic Leu-Val-Glu-Ser-Ser. With the [beta Phe5,8]-bradykinin a mixed sensitizing/potentiating effect was observed, suggesting that a separation of the two effects may be difficult with an intact receptor structure of this kind. This peptide was not hydrolyzed by carboxypeptidase B or chymotrypsin.
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| 3. |
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| 4. |
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| 5. |
- Syvänen, Ann-Christine, et al.
(författare)
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Kininogen in factor VIII-deficient plasma (haemophilia A)
- 1981
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Ingår i: Thrombosis Research. - : Elsevier BV. - 0049-3848 .- 1879-2472. ; 24:4, s. 275-284
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Tidskriftsartikel (refereegranskat)abstract
- The HMr and LMr molecular forms of kininogen were found to occur in normal distribution in plasma from a patient with severe haemophilia A. Present findings indicate that lack of Factor VIII does not influence, the normal content and distribution of immunoreactive kininogens determined by single radial immunodiffusion and radioimmunoassay. The partially purified HMr and LMr kininogens were antigenically identical with the kininogens in normal human plasma determined using the monospecific antisera raised in rabbits against purified kininogen antigens. Low kallikrein activity on H-D-Pro-Phe-Arg-pNA in the haemophilic plasma was apparently due to preparative procedures. This concept is supported by the normal binding ratio of trypsin to pure α2-macroglobulin isolated from the haemophilic plasma.
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| 7. |
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| 8. |
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| 9. |
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| 10. |
- Hamberg, U, et al.
(författare)
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Human kininogen from Cohns Fraction IV : comparisons of antigenicity and multiple forms
- 1979
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Ingår i: Advances in Experimental Medicine and Biology. - 0065-2598 .- 2214-8019. ; 120B, s. 173-183
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Tidskriftsartikel (refereegranskat)abstract
- Kininogen was isolated from Cohns fraction IV by DEAE-chromatography, gel filtration and ammonium sulphate precipitation. Immunologically pure kininogen was prepared by removal of protein impurities using specific immunoadsorbents with Sepharose-bound antibody. Anti-kininogen serum was raised in rabbits against the pure antigen. Comparison with anti-kininogen sera prepared with the biologically active LMW antigen from whole plasma suggested antigenic identity by double immunodiffusion analysis. The Cohn-kininogen was shown to contain mainly two components (85%) in about equal amounts focusing with peaks at pI 4.2 (42%) and pI 4.3 (43%). These represent apparently structurally altered forms of the native plasma kininogen focusing at pI 4.5-4.6 (54%), which occurred as a minor component (13%).
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