Purification of aspartate aminotransferase from Thermus aquaticus.
A method is described for the purification of the enzyme aspartate aminotransferase from the thermophile Thermus aquaticus. The enzyme has been characterized with respect to its molecular weight on SDS PAGE and by amino acid analysis. Attempts to obtain N-terminal sequence data was unsuccessful, presumably due to a blocked N-terminus. The purified enzyme has been shown to be highly thermostable, having a half life of inactivation of about 6 hours at 100 degrees C, and to have a temperature optimum greater than 95 degrees C.
Walker
J M
JM
Division of Biosciences, University of Hertfordshire, Hatfield, Herts, U.K.
Wang
Y X
YX
D000596:Amino Acids / Q000032:analysis; D001219:Aspartate Aminotransferases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D008970:Molecular Weight; D013696:Temperature; D013824:Thermus / Q000201:enzymology* / Q000254:growth & development
D000596:Amino Acids; D001219:Aspartate Aminotransferases