Browsing by Author "Toogood, Helen S."
Now showing items 1-4 of 4
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Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 å resolution
(Elsevier, 1999)Proteins of the subtilisin superfamily (subtilases) are widely distributed through many living species, where they perform a variety of processing functions. They are also used extensively in industry. In many of these ... -
A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp.
(1995)Bacillus sp. strain Wp22.A1 produced a cell-associated aspartic proteinase which was purified to homogeneity using phenyl-Sepharose (hydrophobic and affinity chromatography) and Mono Q. The proteinase has a molecular mass ... -
Purification and characterization of Ak.1 protease, a thermostable subtilisin with a disulphide bond in the substrate-binding cleft
(2000)Ak.1 protease, a thermostable subtilisin isolated originally from Bacillus st. Ak.1, was purified to homogeneity from the Escherichia coli clone PB5517. It is active against substrates containing neutral or hydrophobic ... -
Thermostable proteases from thermophilic microorganisms
(The University of Waikato, 1998)Two metallo-proteases, EA1 and YP-T proteases from Bacillus st. EA1 and B. caldolyticus st. YP-T, respectively, differ in amino acid sequence by only one residue (Val61 = Gly61 in EA1 and YP-T respectively). Yet EA1 protease ...
