Studies on Collagen in Aquatic Animals-III
On some Physicochemical Properties of the Pepsin Solubilized Collagen of the Dolphin Hide
1967 Volume 33 Issue 3 Pages 217-223
Details
1967 Volume 33 Issue 3 Pages 217-223
The study was carried out to elucidate the chemical composition and physicochemical properties of the hide collagen of the dolphin (Tursiops truncatus). By the electron micrograph, the macrostructure of the fiber was found to be constructed of the net work resembling to that of the cattle hide.
The hide was solubilized by pepsin treatment at 25°C in the buffer of pH 1.5 after the pretreatment such as degreasing (ether and acetone), extracting (0.5M Na-acetate and 0.1% acetic acid) and heat denaturation (at 70°C, 10min. in water). The pepsin solubilized collagen (PSC) was reconstituted by dialysing against 0.02M Na2HPO4. The PSC purified thrice by such method as solubilization and reconstitution was analyzed regarding amino acids, sugars, and amino sugar (Table 1 and 2).
By the viscometry, the intrinsic viscosity and thermal denaturation of the PSC were measured (Fig. 1 and 2) and following results were obtained; [η]: 15.2 dl/g, TD: 31°C, whereas Ts was 59°C.
By the sedimentation analysis of the PSC, the molecular weight was proved to be 350000 in native state, and 130000 (α-component) and 200000 (β-component), respectively in denatured state.
By the starch gel electrophoresis method of Kulson et al. (1964), the PSC was separated to the sub-units of αl, α2, β11, β12 and γ components.
