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Chromatographic studies of human lung elastin digestion products obtained by leucocyte elastase: Comparison between newborn and adult soluble fragments
Author(s) -
Smyrlaki Marie,
Davril Monique,
Hayem Annette
Publication year - 1987
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.1130020204
Subject(s) - elastin , chemistry , chromatography , elastase , size exclusion chromatography , elution , digestion (alchemy) , peptide , fraction (chemistry) , high performance liquid chromatography , amino acid analysis , in vivo , amino acid , biochemistry , enzyme , pathology , biology , medicine , microbiology and biotechnology
Human insoluble elastin was prepared from newborn lungs and digested by leucocyte elastase. The soluble fragments were compared to those obtained from adult lung elastin in a previous work (Smyrlaki et al. , 1986). Gel filtration on a Bio‐Gel P‐100 column of newborn elastin allowed the separation of fraction F 1 N (M r 's 30 000–10 000) which was eluted later than the excluded fraction F 1 A (M r 's 80 000–30 000) previously isolated from adult elastin. The difference in the sizes of the large peptide fragments originating from both elastins was also shown on SDS‐PAGE. Reversed phase HPLC was performed on a C 18 column using a multi‐step gradient elution procedure. Different patterns were observed for the high (F 1 N) and the low (F 2 N) molecular size fragments of newborn elastin. The same peak distribution was obtained with adult elastin. Comparison of the amino acid compositions of the most retained peaks (3, 4 and 5), derived from fractions F 1 N and F 1 A, showed analogies for the contents of the major nonpolar amino acids and crosslinks. Thus, this procedure allowed the separation of typical fragments of elastin which might be released in vivo by leucocyte elastase during pulmonary diseases.