| Abstract: | A collagenous glycoprotein (Mr 140000) was isolated from dissociative extracts of foetal bovine nuchal ligament and purified by a combination of ion-exchange and gel-filtration chromatography. This glycoprotein (designated MFPI) exists as a large-Mr disulphide-bonded aggregate in the absence of a reducing agent. The purified glycoprotein was shown to contain about 6% (w/w) carbohydrate, mostly as galactose, glucose and mannose. Amino acid analysis showed the presence of hydroxyproline and hydroxylysine, indicative of its collagenous nature. The collagenous nature of this glycoprotein was further investigated by enzyme digestion. Pepsin digestion produced three major fragments, which were identical with peptides of type VI collagen. Bacterial-collagenase digestion of the unreduced glycoprotein also produced several discrete peptides. However, reduction of the glycoprotein before bacterial-collagenase digestion resulted in the degradation of these discrete peptides. Glycoprotein MFPI extracted in dissociative conditions appears to be a larger-Mr form of type VI collagen, believed to originate from microfibrillar components in the intact tissue. |
