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Role of arg-410 and tyr-411 in human serum albumin for ligand binding and esterase-like activity.
- H. Watanabe, S. Tanase, K. Nakajou, T. Maruyama, U. Kragh-Hansen, M. Otagiri
- Chemistry, BiologyThe Biochemical journal
- 1 August 2000
In addition to its unique ligand binding properties, HSA also possesses an esterase-like activity, and studies with p-nitrophenyl acetate as a substrate showed that, although Arg-410 is important, the enzymic activity of HSA is much more dependent on the presence of Tyr-411.
Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants.
- H. Watanabe, U. Kragh-Hansen, M. Otagiri
- Chemistry, BiologyThe Biochemical journal
- 1 July 2001
The findings show that Trp-214 is not as essential for the high-affinity binding of warfarin as has previously been thought.
Characterization of a binding site of UCN-01, a novel anticancer drug on alpha-acid glycoprotein.
- N. Kurata, S. Matsushita, M. Otagiri
- Chemistry, BiologyBiological & pharmaceutical bulletin
- 1 July 2000
The data suggest that the binding site of UCN-01 on the AGP partly overlaps the binding sites for basic drugs, acidic drugs, as well as steroid hormones.
Arginine 485 of human serum albumin interacts with the benzophenone moiety of ketoprofen in the binding pocket of subdomain III A and III B.
- K. Kaneko, V. Chuang, M. Otagiri
- Chemistry, BiologyDie Pharmazie
- 21 June 2012
LC/Q-TOF mass spectrometry determination revealed that R485 was the amino acid residue that formed covalent adduct with the benzophenone moiety of KP, but not vital to hold KP in the binding pocket of subdomain IIIA.
The development of luminaire for compact self-ballasted fluorescent lamps
- H. Watanabe, T. Maruyama
- Physics
- 1999
A Modification of Mayer's Tannic Acid-Ferric Chloride Staining Method for Demonstrating Cellular Membranous Systems for Light Microscopy
- S. Matsui, K. Hatanaka, H. Watanabe, Y. Asano, H. Yamagata, T. Maruyama
- Biology, MedicineBiotechnic & histochemistry : official…
- 1 January 2000
The modified tannic acid-ferric chloride (MTA-Fe) stain method is a convenient method to visualize cellular membranous systems even for light microscopy and has the advantages of using no toxic materials, simple and easy technique, little variation of staining results, and little fading for several months after staining.