Biomaterial Database

Isolation of the C-terminal peptides of rabbit skeletal myosin. 1978

F Fábián, and L Szilágyi

Purified LMM and its tryptic fragments (LF-1, LF-2 and LF-3) were treated with carboxypeptidase-A and the liberated amino acids were identified by thin layer ion-exchange charomatography. In each protein the only detectable amino acid was leucine. From the total tryptic digest of LMM the C-terminal leucine containing peptides were isolated. Two peptides were found with the following amino acid composition: asx1, g1x6, ala1, leu3, and g1n2-3, leu1, respectively. We obtained the same two peptides from the total tryptic digest of LF-3. We conclude that the C-terminal amino acid of the myosin heavy chain is leucine rather than isoleucine as suggested earlier. Heterogeneity of isolated C-terminal peptides might indicate a heterogeneity in the myosin heavy chains.

UI	MeSH Term	Description	Entries
D007930	Leucine	An essential branched-chain amino acid important for hemoglobin formation.	L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer
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
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
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
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
D015879	Myosin Subfragments	Parts of the myosin molecule resulting from cleavage by proteolytic enzymes (PAPAIN; TRYPSIN; or CHYMOTRYPSIN) at well-localized regions. Study of these isolated fragments helps to delineate the functional roles of different parts of myosin. Two of the most common subfragments are myosin S-1 and myosin S-2. S-1 contains the heads of the heavy chains plus the light chains and S-2 contains part of the double-stranded, alpha-helical, heavy chain tail (myosin rod).	Actomyosin Subfragments,Meromyosin Subfragments,Myosin Rod,Myosin S-1,Myosin S-2,ATPase, Actin-S1,Actin S1 ATPase,Actoheavy Meromyosin,Actomyosin Subfragment 1 ATPase,H-Meromyosin,Heavy Meromyosin,Heavy Meromyosin Subfragment-1,Heavy Meromyosin Subfragment-2,Light Meromyosin,Myosin Subfragment-1,Myosin Subfragment-2,ATPase, Actin S1,Actin-S1 ATPase,H Meromyosin,Heavy Meromyosin Subfragment 1,Heavy Meromyosin Subfragment 2,Meromyosin Subfragment-1, Heavy,Meromyosin Subfragment-2, Heavy,Meromyosin, Actoheavy,Meromyosin, Heavy,Meromyosin, Light,Myosin S 1,Myosin S 2,Myosin Subfragment 1,Myosin Subfragment 2,Subfragment-1, Heavy Meromyosin,Subfragment-1, Myosin,Subfragment-2, Heavy Meromyosin,Subfragment-2, Myosin,Subfragments, Actomyosin,Subfragments, Meromyosin,Subfragments, Myosin