Purification and characterization of an alkaline elastase from Myxococcus xanthus

An extracellular elastase, termed Myxococcus xanthus alkaline protease 1 (MAP1), has been purified from M. xanthus DK1622 culture supernatants by a combination of ion-exchange and affinity chromatographies. It consists of a single peptide chain of 39 kDa. The elastolytic activity was totally suppres...

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Veröffentlicht in:	European journal of biochemistry 1994-08, Vol.223 (3), p.775-782
Hauptverfasser:	Dumont, L, Verneuil, B, Wallach, J, Julien, R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Caseins - metabolism characterization Elastin - metabolism elastolytic activity enzyme activity Gram-negative bacteria Hot Temperature Hydrogen-Ion Concentration Insulin - metabolism Molecular Sequence Data Myxococcus xanthus Myxococcus xanthus - enzymology Pancreatic Elastase - antagonists & inhibitors Pancreatic Elastase - chemistry Pancreatic Elastase - isolation & purification Pancreatic Elastase - metabolism physicochemical properties Protein Denaturation proteinases purification Sequence Analysis soil bacteria Substrate Specificity
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