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Literature DB >> 3593248

Actin antibodies. Preparation and characterization of antibodies specific for smooth-muscle actin isoforms.

J C Cavadore, F Martin, B Calas, J Mery, P Berta, Y Benyamin, C Roustan.

Abstract

We have determined the specificity of sera elicited by glutaraldehyde-stabilized bovine aortic actin. This modification induces a high titre of antibodies directed against the N-terminal (residues 1-39) and the C-terminal region of smooth-muscle actins. The crude antisera were purified on peptide (corresponding to the 1-9 or 1-8 N-terminal sequences of smooth-muscle isoactins)-polyacrylic-resin columns. By fractionating the antisera we obtained oligoclonal antibody populations specific for each isoactin.

Entities: Chemical Gene Species

Mesh：

Substances：
Actins
Antibodies

Year: 1987 PMID： 3593248 PMCID： PMC1147662 DOI： 10.1042/bj2420051

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

19 in total

1. Organic solvents and temperature effects on desorption from immunoadsorbents. DNP-BSA anti-DNP as a model.

Authors: K Andersson; Y Benyamin; P Douzou; C Balny
Journal: J Immunol Methods Date: 1978 Impact factor: 2.303

2. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides.

Authors: E Kaiser; R L Colescott; C D Bossinger; P I Cook
Journal: Anal Biochem Date: 1970-04 Impact factor: 3.365

3. Induction by chemically modified actin derivatives of antibody specificity. A relation between modified sites and antibody interactions with monomeric and filamentous actins.

Authors: Y Benyamin; C Roustan; M Boyer
Journal: FEBS Lett Date: 1983-08-22 Impact factor: 4.124

4. Purification of muscle actin.

Authors: J D Pardee; J A Spudich
Journal: Methods Enzymol Date: 1982 Impact factor: 1.600

5. Refinement of the coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for less than or equal to 0.5 to 50 microgram of protein.

Authors: T Spector
Journal: Anal Biochem Date: 1978-05 Impact factor: 3.365

6. The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation.

Authors: J Vandekerckhove; K Weber
Journal: Differentiation Date: 1979 Impact factor: 3.880

7. Actin typing on total cellular extracts: a highly sensitive protein-chemical procedure able to distinguish different actins.

Authors: J Vandekerckhove; K Weber
Journal: Eur J Biochem Date: 1981-01

Actin antibodies. Preparation and characterization of antibodies specific for smooth-muscle actin isoforms.

1. Organic solvents and temperature effects on desorption from immunoadsorbents. DNP-BSA anti-DNP as a model.

2. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides.

3. Induction by chemically modified actin derivatives of antibody specificity. A relation between modified sites and antibody interactions with monomeric and filamentous actins.

4. Purification of muscle actin.

5. Refinement of the coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for less than or equal to 0.5 to 50 microgram of protein.

6. The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation.

7. Actin typing on total cellular extracts: a highly sensitive protein-chemical procedure able to distinguish different actins.

8. Separation and identification of the major constituents of cytoplasmic gels from macrophages.

9. Cleavage of actin by thrombin.

10. Comparison of purified anti-actin and fluorescent-heavy meromyosin staining patterns in dividing cells.

1. Comparative study of invertebrate actins: antigenic cross-reactivity versus sequence variability.

2. Structural and functional variations in skeletal-muscle and scallop muscle actins.