Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Agnes M. Kanikula"'
Publikováno v:
Protein Expression and Purification. 18:20-26
alpha-Glucosidases (EC 3.2.1.20) are recognized as important in starch degradation during cereal seed germination. A barley (Hordeum vulgare) alpha-glucosidase expressed in Pichia pastoris was cultured in flasks; however, the yield was low necessitat
Autor:
Hazel M. Holden, Matthew M. Benning, Joshua Sakon, Ivan Rayment, Agnes M. Kanikula, Hans H. Liao
Publikováno v:
Biochemistry. 32:11977-11984
Kanamycin nucleotidyltransferase, as originally isolated from Staphylococcus aureus, inactivates the antibiotic kanamycin by catalyzing the transfer of a nucleotidyl group from nucleoside triphosphates such as ATP to the 4'-hydroxyl group of the amin
Autor:
Hans H. Liao, Agnes M. Kanikula
Publikováno v:
Current Microbiology. 21:301-306
Recombinant plasmids carrying either the wildtype kanamycin nucleotidyltransferase gene encoded originally by the mesophilic plasmid pUB110 or the gene encoding the thermostable TK101 mutant were constructed and introduced intoBacillus stearothermoph
Publikováno v:
Archives of biochemistry and biophysics. 295(1)
A thermostable mutant of kanamycin nucleotidyltransferase isolated by cloning and selection for kanamycin resistance in Bacillus stearothermophilus at 70 °C has been crystallized in a form suitable for high-resolution diffraction analysis. This enzy