水産動物のコラーゲンに関する研究-III

ペプシンで可溶化されたイルカ皮コラーゲンの2, 3の物理化学的性質について

抄録

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, T_D: 31°C, whereas T_s 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 α_l, α₂, β₁₁, β₁₂ and γ components.