Abstract
Bovine and chicken bone collagens have been solubilized and presumably denatured (gelatin) by treatment of demineralized, powdered tissue with 70% formic acid. Short periods of extraction such as four hours at 30°, conditions commonly used during cyanogen bromide cleavage of collagen, solubilized 50% and 15% of the chicken and bovine bone collagens respectively. Treatment of the tissues with sodium borohydride partially inhibited the extraction of collagen from chicken bone, but had little effect on the extraction of calf bone collagen. The heterogeneity of the bone gelatin from both species on disc electrophoretic analysis suggested that peptide bonds had been cleaved in some of the collagen chains during exposure to formic acid, thus facilitating the solubilization of the bone collagen as the gelatin. Analysis of the collagen extracted from chicken bone for reducible crosslinks indicated that a large proportion of these bonds had remained intact, in contrast to a previous finding that most of these crosslinks were destroyed in bone gelatin extracted by 4 M CaCl2, at pH 7.0. The stability of the major reducible crosslinks in bone collagen to severe acid conditions may explain in part some of its unique properties, such as its failure to swell or be solubilized in dilute acid, which distinguish it from soft tissue collagens.
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Eyre, D.R., Glimcher, J. The dissolution of bovine and chicken bone collagens in concentrated formic acid. Calc. Tis Res. 15, 125–132 (1974). https://doi.org/10.1007/BF02059050
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DOI: https://doi.org/10.1007/BF02059050