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© Research
Publication : Protein expression and purification

Aspergillus fumigatus metalloproteinase that hydrolyses native collagen: purification by dye-binding chromatography

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Protein expression and purification - 01 Feb 1994

Ibrahim-Granet O, Bertrand O, Debeaupuis JP, Planchenault T, Diaquin M, Dupont B

Link to Pubmed [PMID] – 8167478

Protein Expr. Purif. 1994 Feb;5(1):84-8

A proteinase was purified from the human pathogenic fungus Aspergillus fumigatus. The four chromatographic steps, a “negative” dye column, a “positive” dye column, hydroxyapatite Ultrogel, and modified TSK gel (HW 55), gave a 14% overall yield. The protein migrated as a single band on SDS-PAGE and isoelectric focusing, with an M(r) of 82,000 and a pI of 5.6. Inhibitor studies suggested that the enzyme was a metalloproteinase. It hydrolyzed phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg and cleaved native rat type I collagen.

http://www.ncbi.nlm.nih.gov/pubmed/8167478