Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1988.tb13809.x/fullpdf
Reference32 articles.
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2. Heat-Stable and Fructose 1,6-Bisphosphate-Activated L-Lactate Dehydrogenase from an Extremely Thermophilic Bacterium1
3. l-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium. Desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence
4. Fructose 1,6-Bisphosphate-Dependent L-Lactate Dehydrogenase from Thermus aquaticus YT-1, an Extreme Thermophile: Activation by Citrate and Modification Reagents and Comparison with Thermus caldophilus GK24 L-Lactate Dehydrogenase
5. Nucleotide sequence and characteristics of the gene for l-lactate dehydrogenase of Thermus caldophilus GK24 and the deduced amino-acid sequence of the enzyme
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