Abstract
Seventeen peptides have been isolated from a tryptic digest of soluble elastin by ion exchange chromatography and gel filtration. Molecular weights range from approximately 1,700 to 10,500. Partial or complete amino acid sequences of the peptides were obtained and provide the first extensive data on the primary sequence of elastin. Several important findings stand out. First, the sequences obtained reveal an elastin primary structure quite distinct from collagen and possessing repeats of a tetrapeptide, Gly-Gly-Val-Pro, a pentapeptide, Pro-Gly-Val-Gly-Val, and a hexapeptide, Pro-Gly-Val-Gly-Val-Ala. Second, several of the peptides contain a partial hydroxylation of proline residues thereby definitely establishing hydroxyproline as a real constituent of the elastin chain.
Highlights
Initial separation of the tryptic digest was accomplished by ion exchange chromatography on Technicon Peptide Resin em
We find in the present work that glycines in elastin are not subject to this constraint, so there is not the strict triplet repeat
We find repetitions of a tetrapeptide (Gly-Gly-Val-Pro; in peptide T15, and the NH, terminus of the protein3), of a pentapeptide
Summary
Soluble elastin, isolated from the aortas of copper-deficient swine, was prepared according to the method of Sandberg et al [11]. Initial separation of the tryptic digest was accomplished by ion exchange chromatography on Technicon Peptide Resin em-. Orders for supplementary material should specify the title, authors, and reference to this paper and the JBC Document number, the form desired (microfiche or photocopy), and the number of copies desired. Orders should be addressed to the Journal of Biological. 9650 Rockville Pike, Bethesda, Md. 20014, and must be accompanied by remittance to the order of the Journal in the amount of $2.50 per microfiche or $3.60 per photocopy. AMINO ACID COMPOSITIONS TABLE I OF PURIFIED. TRYPTIC PEPTIOES FROM TROPOELASTIN.a PEPT I DES AMINO
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