Effect of Ca2+ binding to 5,5'-dithiobis(2-nitrobenzoic acid) light chains on conformational changes of F-actin caused by myosin subfragment-1. 1982

Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov

The fluorescent ADP analogue, 1:N6-ethenoadenosine 5'-diphosphate, was incorporated into F-actin in a myosin-free ghost single fibre. Polarized fluorescence measurements of tryptophan residues and 1:N6-ethenoadenosine 5'-diphosphate were performed under a microspectrophotometer to investigate the conformation of F-actin and the changes induced in it by myosin subfragment-1 with 5,5'-dithiobis(2-nitrobenzoic acid) light chains and without them. A relation was found between the conformational state of F-actin and the presence of 5,5'-dithiobis(2-nitrobenzoic acid) light chains. The conformational changes were shown to be controlled by Ca2+ in the presence of 5,5'-dithiobis(2-nitrobenzoic acid) light chains.

UI MeSH Term Description Entries
D009218 Myosins A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D009579 Nitrobenzoates Benzoic acid or benzoic acid esters substituted with one or more nitro groups. Nitrobenzoic Acids,Acids, Nitrobenzoic
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
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
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
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
D002621 Chemistry A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
D004228 Dithionitrobenzoic Acid A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate. 5,5'-Dithiobis(2-nitrobenzoic Acid),DTNB,Ellman's Reagent,5,5'-Dithiobis(nitrobenzoate),Acid, Dithionitrobenzoic,Ellman Reagent,Ellmans Reagent,Reagent, Ellman's
D000199 Actins Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin

Related Publications

Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
November 1983, European journal of biochemistry,
Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
October 1992, Biochemical and biophysical research communications,
Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
May 1984, Biokhimiia (Moscow, Russia),
Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
January 1993, FEBS letters,
Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
September 1967, Biochemical and biophysical research communications,
Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
January 2004, Tsitologiia,
Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
April 1979, Analytical biochemistry,
Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
May 1984, Journal of biochemistry,
Y S Borovikov, and D I Levitskii, and V P Kirillina, and B F Poglazov
February 1981, The Biochemical journal,
Copied contents to your clipboard!