The amino acid sequence of actin from chicken skeletal muscle actin and chicken gizzard smooth muscle actin
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چکیده
منابع مشابه
Actin isoform compartments in chicken gizzard smooth muscle cells.
Differentiated smooth muscle cells typically contain a mixture of muscle (alpha and gamma) and cytoplasmic (beta and gamma) actin isoforms. Of the cytoplasmic actins the beta-isoform is the more dominant, making up from 10% to 30% of the total actin complement. Employing an antibody raised against the N-terminal peptide specific to beta-actin, which labels only the beta-isoform on two-dimension...
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The complete amino-acid sequence of actin of rabbit skeletal muscle was determined. The actin polypeptide chain is composed of 374 residues, including one residue of the unusual amino acid N(r)-methyl histidine, and has a calculated molecular weight of 41,785. The sequence of actin was determined by isolating the peptides produced by cleavage of the protein with cyanogen bromide, determining th...
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The complete amino acid sequence of chicken skeletal-muscle enolase, comprising 433 residues, was determined. The sequence was deduced by automated sequencing of hydroxylamine-cleavage, CNBr-cleavage, o-iodosobenzoic acid-cleavage, clostripain-digest and staphylococcal-proteinase-digest fragments. The presence of several acid-labile peptide bonds and the tenacious aggregation of most CNBr-cleav...
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Abstract Introduction: Myofibroblasts are the main stromal components that constitute the desmoplastic reaction of host cells to inductive stimuli exerted by tumor cells. The purpose of this study was to evaluate the score of myofibroblasts using α -smooth muscle actin marker (α–SMA) in mucoepidermoid carcinoma (MEC) in comparison with pleomorphic adenoma (PA)and study the amount presence of t...
متن کاملStudies on the soluble phosphodiesterases of chicken gizzard smooth muscle.
In this study we describe the identification of four soluble forms of cyclic nucleotide phosphodiesterase from chicken gizzard smooth muscle. These isoenzymes were separated from one another by ion-exchange chromatography on DEAE-cellulose and by calmodulin-Sepharose affinity chromatography. Each form migrates as a single discrete band when it is electrophoresed on non-denaturing polyacrylamide...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1979
ISSN: 0014-5793
DOI: 10.1016/0014-5793(79)80004-6