鯨コラーゲンのSubunitsについて

抄録

The subunits of neutral salt soluble collagen from nose cartilage and pepsin-solubilized collagen from skin of sperm whale were separated by CM-cellulose column chromatography of the denatured proteins and each fraction obtained was examined by disc electrophoresis. For comparison, acid soluble collagen of the great blue shark skin was also studied. The shark collagen consists of α₁, α₂, β₁₁, β₂₂, and γ components and the whale skin collagen consists of α₁, α₂., α₃, β₂₂, γ, and unidentified β (perhaps β₁₁, β₁₃, or β₃₃). As a whole, the chromatograms of these two collagens are similar to those of other reported collagens. However, the chromatogram of collagen from whale nose cartilage was quite different from that of ordinary collagen. When this collagen was chromatographed under similar conditions used for shark and whale skin collagens, protein peaks were very fast in appearing in the effluent, and major parts of the collagen were found to be not adsorbed by CM-cellulose. At a lower ionic strength, four kinds of α and one of β were isolated. The fast peak (α-component) accounted for about 1/3 of the total protein contained 9% hydroxyproline and 2.3% glucuronic acid. This unusual pattern is probably due to the non-coIlagenous material, such as glucuronic acid, combined to the cartilage collagen molecule.