DOI: 10.1111/j.1432-1033.1985.tb09298.x. Bovine serum brevin

Bovine serum brevin

10.1111/j.1432-1033.1985.tb09298.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

Brevin, an actin‐severing protein present in serum from numerous mammals, has been purified to homogeneity from bovine serum, using hydrophobic chromatography as the last purification step. The physicochemical parameters of brevin have been established and some of them studied in the absence and presence of Ca2+. Brevin exhibits an apparent Stokes radius, RS, of 3.4 nm, an intrinsic sedimentation coefficient S°20, w, of 4.8 S and 4.4 S in the absence and presence of Ca2+ respectively, indicative of calcium‐induced conformational change. The native molecular mass of brevin was found to be 68 kDa and the hydrodynamic data suggest that the protein is an asymmetric molecule. Sedimentation equilibrium studies demonstrated that Ca2+ affects the shape (asymmetry) of brevin without altering its molecular mass. Limited tryptic and chymotryptic digestion of brevin distinguishes the Ca2+‐induced conformation from the EGTA one. No change in the electrophoretic migration of brevin was seen upon Ca2+ addition. Several isoforms were detected by two‐dimensional gel electrophoresis. Brevin increases the rate of nucleation of actin but decreases the rate of elongation of the filaments and the steady‐state viscosity of F‐actin in substoïchiometric amounts, as measured by viscometric assays under high shear conditions. Electron microscopic examination documents these effects. Brevin produces shorter actin filaments and binds to the ‘barbed’ end of filaments to which monomers add preferentially during elongation, as demonstrated by indirect immunogold staining of antibodies against brevin. Filament elongation occurs only at the slowly growing end. An enzyme‐linked immunosorbent assay was developed and used to detect and quantify brevin and related proteins in extracts of different bovine cells and tissue. Liver and smooth muscles were found to contain the highest amounts of the severing protein.

Bibliography

SOUA, Z., PORTE, F., HARRICANE, M., FEINBERG, J., & CAPONY, J. (1985). Bovine serum brevin. European Journal of Biochemistry, 153(2), 275â287. Portico.

Authors 5

Zohra SOUA (first)
Francoise PORTE (additional)
Marie‐Cecile HARRICANE (additional)
Jeanne FEINBERG (additional)
Jean‐Paul CAPONY (additional)

References 62 Referenced 36

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Dates

Type	When
Created	20 years, 5 months ago (March 3, 2005, 7:12 p.m.)
Deposited	1 year, 9 months ago (Nov. 23, 2023, 7:13 a.m.)
Indexed	11 months, 3 weeks ago (Sept. 5, 2024, 8:04 a.m.)
Issued	39 years, 8 months ago (Dec. 1, 1985)
Published	39 years, 8 months ago (Dec. 1, 1985)
Published Online	20 years, 5 months ago (March 3, 2005)
Published Print	39 years, 8 months ago (Dec. 1, 1985)

Funders 0

None

BibTeX

@article{SOUA_1985, title={Bovine serum brevin: Purification by hydrophobic chromatography and properties}, volume={153}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1985.tb09298.x}, DOI={10.1111/j.1432-1033.1985.tb09298.x}, number={2}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={SOUA, Zohra and PORTE, Francoise and HARRICANE, Marie‐Cecile and FEINBERG, Jeanne and CAPONY, Jean‐Paul}, year={1985}, month=dec, pages={275–287} }

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      "URL": "https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1985.tb09298.x"
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  "subtitle": [
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