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Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin.

Open access
Balian, G., Click, E.M., Crouch, E., Davidson, J.M., Bornstein, P.·1979·Journal of Biological Chemistry

Abstract

Limited proteolytic cleavage of fibronectin and plasma cold-insoluble globulin with cathepsin D produced two major fragments. The smaller, Mr = 72,000 fragment bound to collagen and contained most of the cysteine in the molecule. This region contains intrachain disulfide bonds which maintain a conformation that is necessary for interaction with collagen. Cleavage of the intact protein and the 72,000-dalton fragment with plasmin localized the collagen-binding region in cold-insoluble globulin to a sequence of about 42,000 daltons. This region is located approximately two-thirds of the linear distance from the NH2 terminus of each chain in the dimeric molecule.

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Metadata

Authors
Balian, G., Click, E. M., Crouch, E., Davidson, J. M., & Bornstein, P.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1979-03
Volume
254
Issue
5
Pages
1429-1432
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1560078646
Cited by
205
References
0
FWCI
18.74
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin. https://app.cochat.ai/papers/10.1016/s0021-9258(17)37782-7
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Balian, G., Click, E. M., Crouch, E., Davidson, J. M., & Bornstein, P. (1979). Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)37782-7

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.