Summary
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1.
The fibrinopeptides A and B from 125 persons were isolated and subjected to careful amino acid analysis.
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2.
All 125 fibrinogen preparations were fully clottable. There was no evidence for any variant molecules being overlooked in a heterozygote by virtue of their not being clotted by thrombin.
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3.
The electrophoretic patterns of 115 sets of fibrinopeptides were all similar within the limits of experimental error. 10 other sets were subjected to (Dowex 50) gradient ion exchange chromatography instead of electrophoresis. All 10 sets had identical eluting profiles, within experimental limits.
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4.
Amino acid analyses of all 125 sets of peptides (125 of A, 125 of B) revealed no differences, even though the precision and sensitivity were more than sufficient to detect the presence of substitutions at the heterozygote level, i.e., ± 0.5 residues/mole peptide.
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5.
The data were carefully evaluated to ensure validity, various degrees of confidence being expressed about various theoretical variations. For example, it is possible that a change of aspartic acid to asparagine at position A 15 might have gone undetected by this procedure, but it seems quite impossible that a change of alanine to threonine at A 7 could have been missed.
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This study was supported by American Heat Association Grant 67, 624 and National Science Foundation Grant GB-4619.
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Doolittle, R.F., Chen, R., Glasgow, C. et al. The molecular constancy of fibrinopeptides A and B from 125 individual humans. Humangenetik 10, 15–29 (1970). https://doi.org/10.1007/BF00297636
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DOI: https://doi.org/10.1007/BF00297636