Biomaterial Database

Comparison of myosin isoenzymes from slow-tonic and fast-twitch fibers of frog muscle. 1981

B Pliszka, and H Strzelecka-Gołaszewska, and C Pantaloni, and A d'Albis

Myosin from distal cruralis bundle of triceps femoris composed of slow-tonic and fast-twitch fibers in an about 1 to 1 ratio, from rectus abdominis containing a lower proportion of slow-tonic fibers, and from a fast-twitch sartorius muscle of the frog, was characterized by means of polyacrylamide gel electrophoresis in the presence of sodium dodecylsulphate (SDS), electrophoresis in non-dissociating conditions, and determination of the ATPase activity. SDS-polyacrylamide gel electrophoresis failed to reveal the presence of any specific light chain in myosin from slow-tonic fibers. Light chains having the same mobilities as fast-twitch LC1 and LC2 were observed; as previously described by Focant and Reznik [15], myosin from tonic fibers appears, on the other hand, devoid of LC3. By electrophoresis in non-dissociating conditions myosin from sartorius muscle was resolved into three components which comigrated with the three myosin isoenzymes from the fast-twitch posterior latissimus dorsi muscle of the chicken. Preparations from rectus abdominis and from cruralis bundle were shown to contain an additional component of lower electrophoretic mobility. Its relative proportion in these two muscles suggests that it represents the slow-tonic fiber myosin isoenzyme. Analysis of proteolytic digestion patterns revealed differences in the heavy chain structure of the isoenzymes from slow and fast fibers, respectively. As indicated by ATPase measurements, fast-twitch myosin exhibits a higher catalytic activity than myosin from slow-tonic fibers, the difference being of the same order as that reported for myosins from slow and fast muscles of higher vertebrates.

UI	MeSH Term	Description	Entries
D007527	Isoenzymes	Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.	Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D009119	Muscle Contraction	A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments.	Inotropism,Muscular Contraction,Contraction, Muscle,Contraction, Muscular,Contractions, Muscle,Contractions, Muscular,Inotropisms,Muscle Contractions,Muscular Contractions
D009132	Muscles	Contractile tissue that produces movement in animals.	Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
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
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011893	Rana esculenta	An edible species of the family Ranidae, occurring in Europe and used extensively in biomedical research. Commonly referred to as "edible frog".	Pelophylax esculentus
D000205	Actomyosin	A protein complex of actin and MYOSINS occurring in muscle. It is the essential contractile substance of muscle.
D000251	Adenosine Triphosphatases	A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.	ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
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