Aspergillus fumigatus metalloproteinase that hydrolyses native collagen: purification by dye-binding chromatography.
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.
Ibrahim-Granet
O
O
Institut Pasteur, Unité de Mycologie, Paris, France.
Bertrand
O
O
Debeaupuis
J P
JP
Planchenault
T
T
Diaquin
M
M
Dupont
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001232:Aspergillus fumigatus / Q000201:enzymology*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D003094:Collagen / Q000378:metabolism; D017364:Collagenases / Q000302:isolation & purification* / Q000378:metabolism; D004396:Coloring Agents; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D007525:Isoelectric Focusing; D008666:Metalloendopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D051381:Rats
D004396:Coloring Agents; D005656:Fungal Proteins; D003094:Collagen; D017364:Collagenases; D008666:Metalloendopeptidases