Isolation of soluble elastin from lathyritic chicks. Comparison to tropoelastin from copper deficient pigs

Abstract

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.

Alternative splicing of human elastin mRNA indicated by sequence analysis of cloned genomic and complementary DNA.

“…An aminoterminal signal sequence (Fig. 3) can be identified by comparison with signal sequences determined in ovine (12) and chick-pretropoelastin (11) and by comparison with the aminoterminal sequences of porcine (8) and chick tropoelastin (6). The encoded amino acid sequence of human tropoelastin shows good homology with the sequenced tryptic peptides of porcine tropoelastin, which have been entirely identified and are here ordered ( Figs.…”

“…The individual polypeptide chains in the elastin fibers are covalently connected by crosslinkages derived from the oxidation of lysine residues by a Curequiring enzyme, peptidyl-lysine oxidise (1)(2)(3)(4). The extensive crosslinking results in great insolubility, and substantial determination of elastin primary structure occurred only after the isolation of a soluble polypeptide, designated tropoelastin (Mr ==72,000), from Cu-deficient or lathyritic animals (5,6). Although many of the tryptic peptides derived from tropoelastin have been sequenced, they have not been ordered (7,8).…”

Characterization of two soybean repetitive proline-rich proteins and a cognate cDNA from germinated axes.

“…Elastin is often prepared by extraction in boiling 0.1 N NaOH (Foster, 1982). The process is carried out, however, on an insoluble residue, and there are no indications that the soluble monomer, tropoelastin (Foster et al, 1975), is alkali-resistant. As noted in Figure 2, soybean extensin is readily hydrolyzed by alkali.…”

Eggshell Composition of Squamate Reptiles: Relationship between Eggshell Permeability and Amino Acid Distribution

“…We performed triplicate analyses on each sample. We selected the extracellular, fibrous proline-rich proteins, reptilian elastin and keratin (Sage and Gray, 1979), and avian elastin (Foster et al, 1975) as controls as well as chicken eggshell (Leach et al, 1981), because of the proteinacious, fibrous nature of reptile eggshells (Sexton et al, 1979;Cox et al, 1982;Packard et al, 1982;DeYSalle et al, 1984;Heulin, 1990).…”