Biomaterial Database

Peptide maps of the myosin isoenzymes of Acanthamoeba castellanii. 1979

H Gadasi, and H Maruta, and J H Collins, and E D Korn

Extracts of Acanthamoeba castellanii contain four myosin-like ATPases (Maruta, H., Gadasi, H., Collins, J.H., and Korn, E.D. (1979) J. Biol. Chem. 254, 3624-3630): double-headed Acanthamoeba myosin II and single-headed Acanthamoeba myosins IA, IB, and IC, which have heavy chains of 170,000, 130,000, 125,000, and 130,000 daltons, respectively, as well as different light chains. In the accompanying paper, evidence is presented that suggests that Acanthamoeba myosin IC is the same molecule as Acanthamoeba myosin IA plus a regulatory 20,000-dalton peptide. This conclusion is confirmed by the identity of the peptide maps obtained by limited proteolysis of the heavy chains of Acanthamoeba myosins IA and IC by Staphylococcus aureus V8 protease. However, peptide maps of the heavy chains of Acanthamoeba myosins IA, IB, and II obtained by limited proteolysis by the Staphylococcus protease and chymotrypsin and by chemical cleavage by cyanogen bromide and cyanylation have few, if any, peptides in common. From this evidence, and the enzymatic and subunit data in the accompanying paper, it is concluded that the three Acanthamoeba myosin isoenzymes, IA (IC), IB, and II, are products of different genes.

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
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
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
D010450	Endopeptidases	A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.	Endopeptidase,Peptide Peptidohydrolases
D003486	Cyanides	Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical.	Cyanide,Isocyanide,Isocyanides
D003488	Cyanogen Bromide	Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.	Bromide, Cyanogen
D000656	Amoeba	A genus of ameboid protozoa. Characteristics include a vesicular nucleus and the formation of several PSEUDOPODIA, one of which is dominant at a given time. Reproduction occurs asexually by binary fission.	Ameba
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
D014357	Trypsin	A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.	Tripcellim,Trypure,beta-Trypsin,beta Trypsin