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PMID: 6809413 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Immunological characterization of the 7-S domain of type IV collagens.

Collagen and related research ·Vol. 1 ·No. 5 ·1981-09-00 ·Pages 419-32

Risteli J, Wick G, Timpl R

Abstract

Antisera were raised against the long and short form of mouse and human 7-S collagen and against type IV collagens solubilized by acid extraction or limited digestion with pepsin. All the antisera showed strong binding for 7-S collagen in radioimmunoassays demonstrating that the 7-S domain which serves as a cross-linking region of type IV collagen is the most immunogenic portion of the molecule. Cross-reaction studies and analysis of fragments showed a complex antigenic structure including some determinants common to the long and short form of 7-S collagen and others unique for the long form. Purified antibodies against 7-S collagen reacted in indirect immunofluorescence with almost all basement membranes of the body indicating that the 7-S domain is a common structural element of type IV collagens.

MeSH Terms
Animals Antibodies/analysis Collagen/immunology Cross Reactions Fluorescent Antibody Technique Guinea Pigs Immunodiffusion Mice Pepsin A/metabolism Peptide Fragments/immunology Rabbits Radioimmunoassay
Chemicals
Antibodies Peptide Fragments Collagen Pepsin A
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Risteli J
Wick G
Timpl R
Article Info
Journal
Collagen and related research
Abbr.
Coll Relat Res
ISSN
0174-173X
Published
1981-09-00
Pages
419-32
Language
English
Region
Germany
NLM ID
8102998
Subset
IM
Grants
NIDCR NIH HHS · N01-DE-82412 · United States
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