Connectin, an elastic protein of muscle. Comparative Biochemistry.
Connectin, an elastic protein, was isolated from both skeletal and cardiac muscles of various species of vertebrates, and also from smooth muscles (gizzard) of the chicken. The amino acid compositions of these preparations were very similar. Connectin was also obtained from claw and tail muscles of the crayfish, but preparations from clam adductor muscles and insect thoracic muscles were heavily contaminated with collagen and resilin, respectively. Connectin-like protein was obtained from cell membranes of erythrocytes and fluorescent anti-connectin staining suggested that it is located on the cytoplasmic surface of the membrane. An attempt to isolate an elastic protein from insoluble residues of amoebae of the slime mold and those of bacterial cell body (Salmonella) was inconclusive. The present comparative bio-chemical study has shown that connectin or connectin-like protein is widely distributed in various types of muscles and in some nonmuscle cells.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001001:Anura; D003400:Astacoidea; D049872:Bivalvia; D002347:Carps; D002417:Cattle; D002645:Chickens; D001517:Coleoptera; D004548:Elasticity; D004910:Erythrocyte Membrane / Q000032:analysis; D005455:Fluorescent Antibody Technique; D009124:Muscle Proteins / Q000302:isolation & purification; D009132:Muscles / Q000032:analysis; D009206:Myocardium / Q000032:analysis; D011817:Rabbits; D011892:Rana catesbeiana; D051381:Rats; D013045:Species Specificity; D014426:Turtles
D000596:Amino Acids; D009124:Muscle Proteins