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Peptide antibody specific for the amino terminus of skeletal muscle alpha-actin.
Author(s) -
J. Chloë Bulinski,
Santosh Kumar,
Koiti Titani,
Stephen D. Hauschka
Publication year - 1983
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.80.6.1506
Subject(s) - skeletal muscle , actin , biology , microbiology and biotechnology , peptide , antibody , alpha (finance) , isozyme , myocyte , peptide sequence , actina , biochemistry , enzyme , cytoskeleton , cell , endocrinology , gene , immunology , medicine , construct validity , nursing , patient satisfaction
The NH2-terminal peptide of skeletal muscle alpha-actin (S alpha N peptide), which contains a primary sequence unique to this actin isozyme, was used to prepare an isozyme-specific peptide antibody. S alpha N peptide was purified from chicken breast muscle actin by preparative reverse-phase HPLC and was coupled to hemocyanin. This complex was used to immunize rabbits in order to elicit actin antibodies specific for the skeletal muscle alpha-actin isozyme. The antibody obtained, called S alpha N antibody, was reactive with S alpha N peptide and with skeletal muscle alpha-actin as well as with cardiac muscle alpha-actin. S alpha N antibody did not react with either of the actin isozymes present in smooth muscle (smooth muscle alpha and gamma) or in brain (nonmuscle beta and gamma). S alpha N antibody was used to detect muscle-specific actin in differentiating mouse and human myoblasts by using immunoblots of myoblast extracts and immunofluorescent staining of fixed cells.

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