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...
متن کاملMobility of microinjected rhodamine actin within living chicken gizzard cells determined by fluorescence photobleaching recovery.
Rhodamine-labeled actin microinjected into living embryonic chicken gizzard cells became associated with its characteristic cytoskeletal structures. In these domains the translational diffusion coefficients (D) of rh-actin were determined in vivo by fluorescence photobleaching recovery (FPR) measurements. Two classes of actin molecules with respect to its mobilities were detected: rh-actin with...
متن کاملAdenoviral 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...
متن کاملCooperativity of actin-activated ATPase of gizzard heavy meromyosin in the presence of gizzard tropomyosin.
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 ...
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: Juntendo Medical Journal
سال: 1980
ISSN: 0022-6769,2188-2134
DOI: 10.14789/pjmj.26.158