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- Andersson, Henrik C.M., et al.
(författare)
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Creep crackgrowth in ex service weld metal of 0.5CrMoV
- 1999
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Ingår i: Cape 99.
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Konferensbidrag (refereegranskat)abstract
- Accurate assessment of the integrity of high temperature components will be of ever increasing importance. The reason for this is that many power plants have reached and exceeded their design life and the number of detected defects increases. This is accentuated by the improvement of the methods for non-destructive testing which means that more and smaller defects will be detected. The possibility to assess the influence of defects on the integrity of high temperature components, will be of vital importance to maintain safe and cost effective power plants. The aim of the present work is to increase the understanding of the influence of service exposure on the remaining life of components in a high temperature plant. The investigation aims to creep test exserviceweld material, 14MoV 6 3, from a Swedish power plant. Thematerial has been in service for a period of about 80 000 hours at atemperature of 530-540 °C and with a nominal hoop stress of 52MPa.Both uniaxial and compact tension creep tests have been performedat a temperature of 550 °C. The stress range used was between 130MPa and 170 MPa for the uniaxial creep tests. For the creep crack growth tests the reference stress was ranging between 122 MPa and146 MPa. A remaining life assessment according to the R5 procedure is included, where material data from the present experimental study is used. The analysis suggests that a defect or a crack with a depth of 2 mm and a length of 5 mm can be left unattended for a season of service under the condition that the service parameters are not changed. A comparison with the assessment of cracks, found in the same plant as the material for the experimental studies came from, and their known extension during service, is included. A parametric study where load level and type of initial defect/crack are varied is also included.
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- Johansson, A, et al.
(författare)
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Epitope specificity of monoclonal anticytokeratin antibody TS1
- 1999
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Ingår i: Cancer Res 1999;59:45-51.
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Tidskriftsartikel (refereegranskat)abstract
- Due to their abundance in epithelial cells and deposition in necrotic regions intratumorally, cytokeratins (CKs) have been established as valuable targets for both radioimmunolocalization and radioimmunotherapy. The target epitope for the monoclonal anti-CK8 antibody, TS1, used for both experimental radioimmunolocalization and radioimmunotherapy, was determined by means of synthesis of 96 overlapping peptides that covered the entire CK8 molecule. A highly conserved peptide sequence, spanning amino acids (aa) 343357 and covering the discontinuous epitope in the helical 2B domain, was identified. The epitope retains its helical structure, as shown with circular dichroism spectroscopy, although the length of the peptide (i.e., >20 aa) is crucial for maintenance of immunoreactivity. To determine which aa residues are crucial for binding to the monoclonal antibody, alanine scanning was performed on a 26-mer covering aa 340365, with the sequence RGELAIKDANAKLSELEAALQRAKQ. The 26 modified peptides were evaluated using ELISA and BIAcore technology. The uniqueness of this epitope has been established by data base sequence comparisons
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- Johansson, A., et al.
(författare)
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Epitope specificity of the monoclonal anticytokeratin antibody TS1
- 1999
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Ingår i: Cancer Research. - 0008-5472 .- 1538-7445. ; 59:1, s. 48-51
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Tidskriftsartikel (refereegranskat)abstract
- Due to their abundance in epithelial cells and deposition in necrotic regions intratumorally, cytokeratins (CKs) have been established as valuable targets for both radioimmunolocalization and radioimmunotherapy. The target epitope for the monoclonal anti-CK8 antibody, TS1, used for both experimental radioimmunolocalization and radioimmunotherapy, was determined by means of synthesis of 96 overlapping peptides that covered the entire CK8 molecule. A highly conserved peptide sequence, spanning amino acids (aa) 343-357 and covering the discontinuous epitope in the helical 2B domain, was identified. The epitope retains its helical structure, as shown with circular dichroism spectroscopy, although the length of the peptide (ie., >20 aa) is crucial for maintenance of immunoreactivity. To determine which aa residues are crucial for binding to the monoclonal antibody, alanine scanning was performed on a 26-mer covering aa 340-365, with the sequence QRGELAIKDANAKLSELEAALQRAKQ. The 26 modified peptides were evaluated using ELISA and BIAcore technology. The uniqueness of this epitope has been established by data base sequence comparisons.
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