抄録
An intact proteoglycan was extracted from salmon (Oncorhynchus keta) nasal cartilage containing type II collagen and prepared
using a novel extraction procedure in water containing a sugar fatty acid ester as an edible detergent. This isolation step suppressed
the degradation of the proteoglycan and simultaneously afforded a proteoglycan-type II collagen matrix. The extracted proteoglycan
was purified, and its properties were compared with those prepared via different extraction procedures using gel permeation
chromatography and polyacrylamide gel electrophoresis. Furthermore, the interaction between the purified proteoglycan and human
L-selectin was analyzed using a bio-layer interferometry biosensor assay; the proteoglycan demonstrated strong binding to L-selectin.
