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Purificationand Comparisonof wild typeTripeptidyl Peptidase II withthe variantC28G
2016 (English)Independent thesis Basic level (professional degree), 10 credits / 15 HE creditsStudent thesis
Abstract [en]

Tripeptidyl peptidase II is a gigantic spindle shaped enzyme complex with a size of >4 MDa found in most eukaryotic cells. The main activity of the enzyme is to remove tripeptides from the N-terminal of longer peptides, thereby contributing to the intracellular protein degradation and the formation of peptides for antigen presentation by MHC I. A missense mutation (c. 82T>G, p.Cys28Gly, C28G) in the gene encoding for tripeptidyl peptidase II has been found in siblings with Multiple Sclerosis, therefore it is of great interest to characterize this variant of protein. The aim of this study was to investigate whether the variant C28G was more sensitive to oxidation damage than the wild type enzyme. Enzymes were purified from Escherichia coli bacteria expressing murine tripeptidyl peptidase II. Purification steps used were: nucleic acid and protein precipitation followed by anion chromatography, hydrophobic interaction chromatography and size exclusion chromatography. The purification yielded 108 μg wild type enzyme and 65 μg of the C28G variant both with a purity of approximately 90 %. Stability analysis with various concentrations of dithiothreitol showed no difference in stability between the enzymes.

Place, publisher, year, edition, pages
2016.
Keywords [en]
TPP II - Multiple sclerosis - plasmid transformation - protein purification – enzyme characterization
National Category
Biomedical Laboratory Science/Technology
Identifiers
URN: urn:nbn:se:uu:diva-349035OAI: oai:DiVA.org:uu-349035DiVA, id: diva2:1199278
Educational program
Biomedical Laboratory Science Programme; Biomedical Laboratory Science Programme
Examiners
Available from: 2018-04-20 Created: 2018-04-20 Last updated: 2018-04-20Bibliographically approved

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