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Hokkaido Food Processing Res. Center Hokkaido Jpn | 論文
- Molecular Cloning of the Genes for Pyruvate Kinase of Two Bacilli, Bacillus psychrophilus and Bacillus licheniformis, and Comparison of the Properties of the Enzymes Produced in Escherichia coli
- A Neopullulanase-type α-Amylase Gene from Thermoactinomyces vulgaris R-47
- Application of a Metal Switch to Aqualysin I, a Subtilisin-type Bacterial Serine Protease, to the S3 Site Residues, Ser102 and Gly131
- Identification and Designing of the S3 Site of Aqualysin I, a Thermophilic Subtilisin-Related Serine Protease
- Substrate Specificity of Aqualysin I Altered by an Organic Solvent, DMSO
- Substrate Specificity of Aqualysin I, a Bacterial Thermophilic Alkaline Serine Protease from Thermus aquaticus YT-1 : Comparison with Proteinase K, Subtilisin BPN' and Subtilisin Carlsberg
- P1-Specificity of Aqualysin I (a Subtilisin-type Serine Protease) from Thermus aquaticus YT-1,using P1-Substituted Derivatives of Streptomyces Subtilisin Inhibitor
- Stability of Thermostable Enzyme, Aqualysin I ; a Subtilisin-type Serine Protease from Thermus aquaticus YT-1
- Involvement of NH_2-Terminal Pro-sequence in the Production of Active Aqualysin I (a Thermophilic Serine Protease) in Escherichia coli(Biological Chemistry)
- Molecular Cloning and Nucleotide Sequence of the Aminopeptidase T Gene of Thermus aquaticus YT-1 and Its High-level Expression in Escherichia coli(Microbiology & Fermentation Industry)
- Involvement of Glu-264 and Arg-235 in the Essential Interaction between the Catalytic Imidazole and Substrate for the D-Lactate Dehydrogenase Catalysis
- Expression of Aqualysin I (a Thermophilic Protease) in Soluble Form in Escherichia coli under a Bacteriophage T7 Promoter
- Production of Thermophilic Protease by Clucose-Controlled Fed-Batch Culture of Recombinant Escherichia coli
- Isolation and Characterization of a Thermostable Aminopeptidase (Aminopeptidase T) from Thermus aquaticus YT-1, an Extremely Thermophilic Bacterium(Biological Chemistry)
- Secretion of Human Interleukin-2 in Biologically Active Form by Bacillus brevis Directly into Cultute Medium
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