Characteristics and in vivo occurrence of type VIII collagen

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Abstract
Type VIII collagen was isolated from bovine Descemet''s membranes by pepsin treatment and salt fractionation, as described by Kapoor et al. [(1986) Biochemistry 25, 3930-3937]. Contaminating type IV collagen was removed by ion-exchange chromatography. Purified type VIII collagen consisted of two different polypeptide chains and, compared to the fiber forming collagens, showed a higher thermal stability. Corresponding fractions isolated from pepsinized human Ewing''s sarcoma and fetal calf aorta reacted immunologically with a protein of similar molecular mass. After extraction of Descemet''s membranes with guanidine hydrochloride, a peptide of about 60 kDa was obtained. This seems to be the tissue form of type VIII collagen.