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M Davril

Publications and source records attributed to M Davril.

At least 55 records · Page 3Linked to original sources
PubMed1979

Isolation and characterization of desmosine(s) containing peptide fractions of normal and diseases human aortic elastin.

Normal and diseased human aortic elastins were isolated and highly purified. They were subsequently submitted to elastase and thermolysin digestion followed by partial acid hydrolysis to increase crosslinkage. The peptide fractions containing these highly cross-linked desmosines were extensively purified either by ion exchange chromatography or by gel-filtration. Their amino acid composition was determined. Detailed investigation of the purified peptide fraction from normal human elastin containing desmosines was carried out using different N-terminal and C-terminal procedures, thus permitting the probable covalent structure of the desmosine containing peptide(s) to be proposed. Irrespective of their origin (healthy or pathologic), the elastin samples all revealed the same amino acid composition with a very high alanine content in the cross-linking peptides. This work is submitted as proof that changes in amino acid composition are essentially due to "dilution" and contamination by structural glycoproteins and not to structural changes in amino acid compoistion in the vicinal cross-links positions. We find that not only "clustering" alanine residues but also glycine, proline, valine, leucine and tyrosine residues are located in the immediate vicinity of both desmosine and isodesmosine residues.

Amino Acid Sequence↗
PubMed1979

Guanidination of kappa-elastin from bovine ligamentum nuchae.

Kappa-Elastin is exhaustively guanidinated in order to chemically modify the pre-existing lysine content to homoarginine. However the pre-existing lysine content is only modified to homoarginine content about 50 p.cent. The other lysyl-bonds are buried or/and engaged to aldi-imine bonds or other bonds. Therefore the first guanidinated kappa-Elastin is submitted to partial acide hydrolysis (HCL, 1 N, 110 degrees C for 2 hours) and submitted to a second exhaustive guanidination. The pre-existing lysin content in kappa-Elastin almost quantitively disappeared and is transformed to the corresponding homoarginine. These results are similar to those obtained by photolysis of (Iso) desmosine residues by UV light which will liberate "new" lysine containing peptides from kappa-Elastin.

Amino Acids↗
PubMed1976

Purification of a lysinonorleucine cross-linked peptide fraction from porcine aorta elastin.

Highly purified elastin from porcine aorta was submitted to elastase digestion. The enzymic products were subjected to gel filtration on Sephadex G 25. The excluded fraction was then submitted to thermolysin digestion and gel filtration. The excluded fraction was submitted to partial acid hydrolysis and gel filtration. Several sub-fractions were obtained. The F3 subfraction containing cross-linking agents (desmosines and lysinonorleucine) was finally subjected to ion exchange chromatography. A highly enriched peptide fraction containing lysinomorleucine was obtained and then purified by preparative electrophoresis. The ratio of enrichment passed from 2 residues of lysinonorleucine (expressed as lysine) from starting material (elastin) to 178 out of 1,000 residues in the final step. In this peptide fraction, if we express in molar ratio and consider the amount of lysinonorleucine is one residue, the following amino-acid composition is Pro:3, Gly:1, Ala:2, LNL:1, Lys:2. No traces of desmosines are detected. The role of lysinonorleucine in bridging functions in elastin is discussed.

Amino Acids↗