caa a22 4500 397555814 CHVBK 20180308164801.0 cr unu---uuuuu 161202e199601 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021204 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021204 Gel Formation from the Type IV Collagen Isolated from Bovine Lens Capsule in Guanidine-HCl and Dithiothreitol [Elektronische Daten] [Masatoshi Muraoka, Koichi Nakazato, Toshihiko Hayashi] Type IV collagen was prepared from bovine lens capsule by acetic acid extraction, followed by purification including DEAE-Sephacel chromatography and dialysis. The type IV collagen solution became viscous and eventually gelated upon dialysis against 2 M guanidine-HCl and 10 mM dithiothreitol. Gelation was not observed for heat-denatured type IV collagen, suggesting that collagenous conformation may be required for the gelation. A reducing agent, dithiothreitol, was essential for the gelation of type IV collagen in 2 M guanidine-HCl. An optimal concentration of guanidine-HCl for the gelation lays between 1.5 and 2.5 M: gelation did not occur at 1 M or lower and at 3 M or higher, although the circular dichroism spectrum characteristic of the collagenous triple-helix was not changed in 3 M guanidine-HCl. This suggests that an appropriate change in conformation of the type IV collagen at a region other than the triple-helical region or/and partial dissociation of complexed type IV collagen aggregates may drive intermolecular interactions of the type IV collagen leading to polymerization and eventually to gelation. To our knowledge, this is the first report that the type IV collagen alone has the ability to form a rigid gel. The assembled structure of the type IV collagen in gel form might be related to the skeletal architecture of basement membrane(s). © by the Journal of Biochemistry Regular Papers nationallicence basement membrane nationallicence gel nationallicence guanidine-HCl nationallicence self-assembly nationallicence type IV collagen nationallicence Muraoka Masatoshi Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153 aut Nakazato Koichi Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153 aut Hayashi Toshihiko Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153 aut The Journal of Biochemistry Oxford University Press 119/1(1996-01), 167-172 0021-924X 119:1<167 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021204 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021204 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Muraoka Masatoshi Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153 aut NATIONALLICENCE 700 1- Nakazato Koichi Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153 aut NATIONALLICENCE 700 1- Hayashi Toshihiko Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/1(1996-01), 167-172 0021-924X 119:1<167 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford