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Isolation of Crosslinked Peptides from Insoluble Human Leiomyoma: The Involvement of the N‐Terminal, Non‐helical Region of Type III Collagen in Intermolecular Crosslinking

European Journal of Biochemistry, ISSN: 1432-1033, Vol: 96, Issue: 2, Page: 249-256
1979
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Two collageneous crosslinked peptides have been isolated from tryptic digests of sodium cyanoborohydride(NaBHCN)‐reduced insoluble matrix of human leiomyoma. The amino acid composition of both peptides demonstrates that the N‐terminal, non‐helical region of type III collagen is involved in crosslinking. The monomer (Col1) and dimer (Col1) N‐terminal, non‐helical peptides, consisting of 21 and 42 residues respectively, were found to be cross‐linked to a tryptic peptide ('T9′, 9 residues) from the helical region of an adjacent type III molecule, forming the crosslinked peptides Col1 × T9 and (Col1)× T9. The location of peptide T9 in the C‐terminal, helical crosslink region [residues 922–930 of the α1(III)chain] was confirmed by the following observations. Its amino acid composition, which was deduced by calculation of the composition difference between the crosslinked peptide (Col1)× T9 and the non‐crosslinked peptide (Col1). This was consistent with the corresponding sequence of calf calf α1(III) when methionine is replaced by hydroxyproline. Cleavage of the crosslink of Col 1 × T9 by periodate, which released a peptide with the amino acid composition of T9. Sequence determination of the crosslinked peptide (Col1)× T9; since the N‐terminus of Col1 is blocked by pyroglutamic acid, sequence determination reveals the N‐terminal sequence of T9: (Formula Presented.) The chemical nature of the reduced crosslinks was shown to be different in the two crosslinked peptides. Col1 × T9 contains hydroxylysinonorleucine oLys(ω Nle) whereas (Col1)× T9 contains a trifunctional crosslink, which is different from the trifunctional crosslinks that have been found in type I collagen. Copyright © 1979, Wiley Blackwell. All rights reserved

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