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Title: Amino acid sequence studies of lysyl oxidase and TRAMP (tyrosine rich acidic matrix protein)
Author: Cronshaw, Andrew D.
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1994
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Lysyl oxidase initiates crosslinking in collagens and elastin by the conversion of specific lysine (and, in collagen, hydroxylysine) residues to peptidyl α-aminoadipic-δ-semialdehyde. Porcine skin lysyl oxidase (Mr=34K) and a protein (Mr=24K) with which the enzyme co-purifies have been isolated and characterised. The 24K protein was originally thought to be a degradation product of lysyl oxidase but this study shows it to be a distinct protein. Four variants of lysyl oxidase and five variants of the 24K protein were identified by Mono Q anion-exchange Fast Protein Liquid Chromatography (FPLC). Each lysyl oxidase variant was subjected to amino acid analysis, which did not reveal any differences between variants, and by mass analysis, which showed small incremental changes between the variants. All the 24K protein variants were indistinguishable by amino acid analysis, though the protein was clearly distinct from lysyl oxidase. As with lysyl oxidase however, mass analysis showed small incremental changes between each TRAMP variant. Both lysyl oxidase and the 24K protein were found to be N-terminally blocked. A variety of cleavage methods were employed and the resulting peptides were subjected to mass and sequence analysis. Lysyl oxidase was cleaved using cyanogen bromide and the N-terminal fragment was found and sub-digested with endoproteinase-Asp-N. From these peptides it was possible to suggest the location of the N-terminus of lysyl oxidase. The 24K protein was cleaved with cyanogen bromide and digested with various enzymes which included pyroglutamate aminopeptidase, clostripain, protease V8, and endoproteinase-Asp-N.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available