Purification and characterization of a pepstatin-insensitive, thermostable, extracellular acid proteinase from a bacterium

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dc.contributor.authorPrescott, Mark
dc.contributor.authorPeek, Keith
dc.contributor.authorPrendergast, Elizabeth
dc.contributor.authorDaniel, Roy M.
dc.date.accessioned2010-08-31T05:01:14Z
dc.date.available2010-08-31T05:01:14Z
dc.date.issued1992
dc.description.abstractAspartate proteinases (also referred to as acid or carboxyl) represent one of the four major classes of proteinase. Work on members of this group has centered largely around those enzymes isolated from mammalian, fungal, or plant sources. Some of these have proven to be of great economic importance, for example, the renneting enzyme, chymosin.en_NZ
dc.identifier.citationPrescott, M., Peek, K., Prendergast, E. & Daniel, R.M. (1992). Purification and characterization of a pepstatin-insensitive, thermostable, extracellular acid proteinase from a bacterium. Annuals of the New York Academy of Sciences, 672, 167-170.en_NZ
dc.identifier.doi10.1111/j.1749-6632.1992.tb35619.xen_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4490
dc.language.isoen
dc.publisherWileyen_NZ
dc.relation.urihttp://onlinelibrary.wiley.com/doi/10.1111/j.1749-6632.1992.tb35619.x/abstracten_NZ
dc.subjectproteinasesen_NZ
dc.titlePurification and characterization of a pepstatin-insensitive, thermostable, extracellular acid proteinase from a bacteriumen_NZ
dc.typeJournal Articleen_NZ
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