Glycosylation Patterns on Collagen α1(I) and Collagen α2(I) resemble a lock and key arrangement
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ABSTRACT: Col1 from the skins of 4 animals (cow, deer, goat and sheep) were purified, then used mass spectrometry and proteomic techniques to identify lysines that were oxidised, galactosylated, glucosylgalactosylated, or glycated in its ma-ture sequence. We found 18 out of the 38 lysines in collagen type 1α1, (Col1A1) and 7 of the 30 lysines in collagen type 1α2 (Col1A2) were glycosylated. Six of these modifications had not been reported before, and included a lysine involved in cross linking collagen molecules. Mapping the positions of these modifications on the ColA1 and Col1A2 sequences showed they were complimentary and resembled a lock and key arrangement.
INSTRUMENT(S): Q Exactive
ORGANISM(S): Bos Taurus (bovine) Capra Hircus X Ovis Aries
TISSUE(S): Skin
SUBMITTER: Trevor Loo
LAB HEAD: Gill Norris
PROVIDER: PXD036507 | Pride | 2023-05-24
REPOSITORIES: Pride
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