Open AccessCharacteristics and in vivo occurrence of type VIII collagen
Author(s) -
JANDER Renate,
KORSCHING Eberhard,
RAUTERBERG Jürgen
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb15528.x
Subject(s) - chemistry , guanidine , fractionation , in vivo , molecular mass , membrane , type i collagen , biochemistry , microbiology and biotechnology , collagen fiber , peptide , chromatography , enzyme , anatomy , biology , endocrinology
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.