Involvement of NH2-Terminal Pro-sequence in the Production of Active aqualysin I (a Thermophilic Serine Protease) in Escherichia coli.
Lee YC, Miyata Y, Terada I, Ohta T, Matsuzawa H
Agric. Biol. Chem., 1991
2
A non-covalent NH2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli.
Lee YC, Ohta T, Matsuzawa H
FEMS Microbiol. Lett., 1992
3
Two Step Single Primer Mediated Polymerase Chain Reaction. Application to Cloning of Putative Mouse β-Galactoside α2,6-Sialyltransferase cDNA.
Hamamoto T, Kawasaki M, Kurosawa N, Nakaoka T, Lee YC, Tsuji S
Bioorg. Med. Chem., 1993
4
Phosphatidylserine Specific Binding Protein in Rat Brain: Purification and Characterization.
Nakaoka T, Kojima N, Hamamoto T, Kurosawa N, Lee YC, Kawasaki H, Suzuki K, Tsuji S
J. Biochem., 1993
5
Molecular cloning and expression of the Galβ1,3GalNAc α2,3-Sialyltransferase from mouse brain.
Lee YC, Kurosawa N, Hamamoto T, Nakaoka T, Tsuji S
Eur. J. Biochem., 1993
6
Molecular cloning and Expression of the GalNAc α2,6-Sialyltransferase.
Kurosawa N, Hamamoto T, Lee YC, Nakaoka T, Kojima N, Tsuji S
J. Biol. Chem., 1994
7
Molecular cloning and expression of Chick Embryo Galβ1,4GlcNAc α2,6-Sialyltransferase: Comparison with the Mammalian Enzyme.
Kurosawa N, Kawasaki M, Hamamoto T, Nakaoka T, Lee YC, Arita M, Tsuji S
Eur. J. Biochem., 1994
8
Cloning and Expression of cDNA for a New Type of Galβ1,3GalNAc α2,3-Sialyltransferase.
Lee YC, Kojima N, Wada E, Kurosawa N, Nakaoka T, Hamamoto T, Tsuji S
J. Biol. Chem., 1994
9
Expression of Mouse Galβ1,4GlcNAc α2,6-Sialyltransferase in an Insoluble Form in Escherichia coli and Partial Renaturation.
Hamamoto T, Lee YC, Kurosawa N, Nakaoka T, Kojima N, Tsuji S
Bioorg. Med. Chem., 1994
10
Kinetic Properties and Acceptor Substrate Preference of Two Kinds of Galβ1,3GalNAc α 2,3-Sialyltransferase from Mouse Brain.