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Cited by 283

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Vitamin D-binding protein (Gc-globulin) binds actin.

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Van Baelen, H., Bouillon, R., De Moor, P.·1980·Journal of Biological Chemistry

Abstract

Actin, an ubiquitous highly conserved intracellular protein, and the serum vitamin D-binding protein (DBP) form tight 1:1 molar complexes in vitro. This interaction, which is not species-specific, explains the widespread occurrence of the 5-6 S protein responsible for the binding of 25-hydroxycholecalciferol in high speed supernatants of all nucleated tissues. Incubation of F-actin, the filamentous form of this protein, with DBP leads to depolymerization of the former. Actin, complexed with deoxyribonuclease I, retains its ability to bind DBP. Erythrocyte actin, prepared from red cell ghosts, also displays binding properties for DBP. The biological significance of this new interaction of actin is not yet understood.

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Metadata

Authors
Van Baelen, H., Bouillon, R., & De Moor, P.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1980-03
Volume
255
Issue
6
Pages
2270-2272
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2166659336
Cited by
283
References
0
FWCI
14.65
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Vitamin D-binding protein (Gc-globulin) binds actin. https://app.cochat.ai/papers/10.1016/s0021-9258(19)85885-4
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Van Baelen, H., Bouillon, R., & De Moor, P. (1980). Vitamin D-binding protein (Gc-globulin) binds actin. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)85885-4

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