Structural Analysis of Fibronectin and Its Collagen-Binding Fragment from Several Cell Lines
Tryptic peptide mapping of fibronectin from various species indicates that (i) there exists a remarkable similarity between methionine-labeled tryptic peptides of fibronectins isolated from cells of widely separated species such as human, chicken, mouse, hamster, and rat; (ii) fibronectins from norm...
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Published in: | Proceedings of the National Academy of Sciences - PNAS Vol. 81; no. 1; pp. 28 - 32 |
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Main Author: | |
Format: | Journal Article |
Language: | English |
Published: |
United States
National Academy of Sciences of the United States of America
01-01-1984
National Acad Sciences |
Subjects: | |
Online Access: | Get full text |
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Summary: | Tryptic peptide mapping of fibronectin from various species indicates that (i) there exists a remarkable similarity between methionine-labeled tryptic peptides of fibronectins isolated from cells of widely separated species such as human, chicken, mouse, hamster, and rat; (ii) fibronectins from normal and transformed or tumor cells of the same species are very similar, if not identical; and (iii) collagen-binding regions of fibronectin from different species share identical major peptides. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.81.1.28 |