Isolation of soluble elastin from lathyritic chicks. Comparison to tropoelastin from copper deficient pigs.
Tropoelastin was isolated from the aortas of chicks rendered lathyritic by treatment with beta-aminopropionitrile. The soluble elastin was judged homogeneous by sodium dodecyl sulfate polyacrylamide gel electrophoresis and possessed an estimated molecular weight of 70000. Automated sequential analysis revealed that the N-terminal region of the chick tropoelastin is very homologous to tropoelastin isolated from copper-deficient piglets. N-terminal analysis of a trypsin digest of chick tropoelastin showed that tyrosine frequently is found adjacent to lysine residues. This positioning of tyrosine residues may be significant in terms of a possible regulatory role in elastin cross-link formation.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000032:analysis / Q000378:metabolism; D002645:Chickens; D003300:Copper / Q000172:deficiency*; D004549:Elastin / Q000032:analysis / Q000378:metabolism*; D007842:Lathyrism / Q000378:metabolism*; D008970:Molecular Weight; D011498:Protein Precursors / Q000032:analysis / Q000378:metabolism*; D013552:Swine; D014357:Trypsin
D000596:Amino Acids; D011498:Protein Precursors; D003300:Copper; D004549:Elastin; D014357:Trypsin