Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0271276 (Hudson)
 1,066 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The globular domain of type IV collagen from bovine glomerular basement membrane was isolated under nondenaturing conditions. It was shown to exist in a hexameric form comprising monomeric and dimeric subunits, with the Goodpasture antigen residing in monomer M2 and dimer D2 as previously described (Butkowski, R. J., Wieslander, J., Wisdom, B. J., Barr, J. F., Noelken, M. E., and Hudson, B. G. (1985) J. Biol. Chem. 260, 3739-3747). The epitope, however, is sequestered inside the hexamer, but becomes exposed and binds with the Goodpasture antibody upon dissociation of the hexamer into its subunits after treatment with concentrated guanidine HC1 or dilute acetic acid (pH less than 3.0). The process is completely reversible even from the denatured state. Circular dichroism studies show that the conformation of each subunit is unusually resistant to change in 6 M guanidine HC1 at 25 degrees C. This suggests that exposure of the epitope by dissociation requires minimal or no unfolding of subunits. The results provide additional evidence for localization of the Goodpasture antigen to the globular domain of type IV collagen. Moreover, these studies extend the conclusion (Weber, H., Engel, J., Wiedemann, H., Glanville, R., and Timpl, R. (1984) Eur. J. Biochem. 139, 401-410) about a tumor basement membrane, to an authentic physiological membrane, that the globular domain is a major cross-linking site in the type IV collagen matrix.
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PMID:Physical and immunochemical studies of the globular domain of type IV collagen. Cryptic properties of the Goodpasture antigen. 240 91

The collagenous components of Ascaris suum intestinal basement membrane were isolated by extraction with 0.1 M Tris-HC1, 0.5 M NaC1, 0.5% 2-mercaptoethanol, pH 8.3, and Sephacryl S-300 gel filtration. Rotary-shadowing electron microscopy showed that the collagenous components occur as monomers and dimers with mean contour lengths of 469 +/- 21 and 918 +/- 24 nm, respectively. The molecules each contain a globular domain, with that of the dimer being slightly larger than that of the monomer. Electrophoresis in sodium dodecyl sulfate-polyacrylamide gels under reducing conditions revealed two polypeptides of Mr = 185,000 and 179,000. A similarity to type IV collagen was indicated by a glycine content of less than 33 mol % and the presence of fucose, mannose, and glucosamine residues. Treatment of the collagen with pepsin resulted in loss of the globular domains but retention of 90% of the length of fibrous collagen segments. Collagenase, however, removed the fibrous regions but left the globular moieties intact. These results extend the previously proposed model (Hung, C.-H., Noelken, M. E., and Hudson, B. G. (1981) J. Biol. Chem. 256, 3822-3826) in which the collagenous domain consists of two monomer-sized triple-helical subunits joined end-to-end by disulfide bonds, with the constituent chains of each subunit being cross-linked by disulfide bonds.
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PMID:Intestinal basement membrane of Ascaris suum. Molecular organization and properties of the collagen molecules. 395 13