Purification and characterization of a pepstatin-insensitive, thermostable, extracellular acid proteinase from a bacterium
Prescott, 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.
Permanent Research Commons link: https://hdl.handle.net/10289/4490
Aspartate 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.