Amino acid sequence of chicken gizzard beta-tropomyosin. Comparison of the chicken gizzard, rabbit skeletal, and equine platelet tropomyosins.
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چکیده
منابع مشابه
Adenoviral gizzard erosions in Italian chicken flocks.
TYPE 1 avian adenoviruses belong to the genus Aviadenovirus within the adenovirus family. Five species of fowl adenovirus (fAdV) (designated by the letters A to E) are recognised within the Aviadenovirus genus based largely on molecular criteria, in particular restriction enzyme fragmentation patterns and sequencing data (McFerran and McConnel Adair 2003). fAdV are common infectious agents in p...
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The amino acid sequence of the large cyanogen bromide fragment (residues 11 to 127) derived from the NH,-terminal half of cY-tropomyosin has been determined. This was achieved by automatic sequence analysis of the whole fragment as well as manual sequencing of fragments derived from tryptie digestion of the maleylated fragment and thermolytic, Myxobacter 495 cu-lytic and Staphylococcus aureus p...
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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...
متن کاملThe complete amino acid sequence of chicken skeletal-muscle enolase.
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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The mechanism for the potentiation of the actin-activated ATPase of smooth muscle myosin by tropomyosin is investigated using smooth muscle actin, tropomyosin, and heavy meromyosin. In the presence of tropomyosin, an increase in Vmax occurs with no effect on KATPase and Kbinding at 20 mM ionic strength. Utilizing N-ethylmaleimide-treated subfragment-1, which forms rigor complexes with actin in ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)39602-3