Interaction between chicken gizzard caldesmon and tropomyosin. 1988

T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
Department of Functional Polymer Science, Faculty of Textile Science and Technology, Shinshu University, Nagano.

Chicken gizzard muscle caldesmon has been examined for ability to interact with tropomyosin from chicken gizzard muscle by using fluorescence enhancement of tropomyosin labeled with dansyl chloride (DNS) and affinity chromatography. The binding of caldesmon to tropomyosin was regulated by Ca2+ and calmodulin, i.e., at low ionic strength most of the caldesmon bound to tropomyosin-Sepharose 4B was co-eluted by adding calmodulin only in the presence of Ca2+, but not in its absence. This regulation by Ca2+ and calmodulin was also suggested by fluorescence measurements. Actin- and calmodulin-binding sites on the caldesmon molecule were located in the 38K fragment (Fujii, T., Imai, M., Rosenfeld, G.C., & Bryan, J. (1987) J. Biol. Chem. 262, 2757-2763). When 38K-enriched fraction was applied to the tropomyosin-Sepharose, the 38K fragment was retained by the column and could be eluted by adding Ca2+ and calmodulin.

UI MeSH Term Description Entries
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002147 Calmodulin A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels. Calcium-Dependent Activator Protein,Calcium-Dependent Regulator,Bovine Activator Protein,Cyclic AMP-Phosphodiesterase Activator,Phosphodiesterase Activating Factor,Phosphodiesterase Activator Protein,Phosphodiesterase Protein Activator,Regulator, Calcium-Dependent,AMP-Phosphodiesterase Activator, Cyclic,Activating Factor, Phosphodiesterase,Activator Protein, Bovine,Activator Protein, Calcium-Dependent,Activator Protein, Phosphodiesterase,Activator, Cyclic AMP-Phosphodiesterase,Activator, Phosphodiesterase Protein,Calcium Dependent Activator Protein,Calcium Dependent Regulator,Cyclic AMP Phosphodiesterase Activator,Factor, Phosphodiesterase Activating,Protein Activator, Phosphodiesterase,Protein, Bovine Activator,Protein, Calcium-Dependent Activator,Protein, Phosphodiesterase Activator,Regulator, Calcium Dependent
D002148 Calmodulin-Binding Proteins Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases. Caldesmon,Calspectin,CaM-BP(80),Caldesmon (77),Calmodulin Binding Proteins,Proteins, Calmodulin-Binding
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D003619 Dansyl Compounds Compounds that contain a 1-dimethylaminonaphthalene-5-sulfonyl group. Dimethylaminonaphthalenesulfonyl Compounds,Compounds, Dansyl,Compounds, Dimethylaminonaphthalenesulfonyl
D005895 Gizzard, Avian The posterior portion of the avian stomach located between the PROVENTRICULUS and INTESTINE. It consists of a thick muscular wall and small stones (gastroliths) that function to mechanically grind SEEDS and other ingested objects. Gizzard,Ventriculus,Avian Gizzard,Avian Gizzards,Gizzards,Gizzards, Avian
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013050 Spectrometry, Fluorescence Measurement of the intensity and quality of fluorescence. Fluorescence Spectrophotometry,Fluorescence Spectroscopy,Spectrofluorometry,Fluorescence Spectrometry,Spectrophotometry, Fluorescence,Spectroscopy, Fluorescence

Related Publications

T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
February 1987, The Journal of biological chemistry,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
June 1993, Biological & pharmaceutical bulletin,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
April 1996, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
September 1985, The Biochemical journal,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
June 1987, FEBS letters,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
November 1988, The Biochemical journal,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
February 1998, Tissue & cell,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
June 1984, Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
October 1988, Biochemical and biophysical research communications,
T Fujii, and J Ozawa, and Y Ogoma, and Y Kondo
June 1985, The Journal of biological chemistry,
Copied contents to your clipboard!