Abstract
The acid-extracted collagen of hake swim bladders prepared in highly purified form was characterized by its physicochemical properties and chemical composition. Chemical studies included quantitative amino acid analysis; hexose, aldehyde, and ester-like bond determinations and measurement of relative amounts of α, β, and γ components of the molecule. The unusually low denaturation temperature of 19 ° found for this collagen correlates well with its low content of proline and hydroxyproline, but apparently has no connection with the amount of hexoses, aldehyde groups, and ester-like bonds; furthermore, present data, together with that already existing in the literature, seem to indicate that the stability of the collagen molecule is not dependent on the proportion of β dimers and γ trimers.
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