Purification and Structural Aspects of Type I Collagen from Walleye Pollock (Theragra chalcogramma) Skin

Type I collagen was extracted from walleye pollock (Theragra chalcogramma) skin and purified by DEAE-52 cellulose chromatography and gel filtration chromatography with Sephacryl S-300 HR. Fourier transform infrared spectroscopy spectra and X-ray diffraction pattern showed the existence of a helical arrangement, with the distance between the molecular chains of 1.18 nm and the unit height, typical of the triple helix, of 0.27 nm. Scanning electron microscopy (SEM) revealed the collagen had a filamentary structure. Peptide mapping, obtained by matrix assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS), indicated that peptides with the molecular weight of 1,470, 1,565, 1,570, 2,150, and 2,470 Da were the major products of trypsin digestion of pollock skin collagen.