Zobrazeno 1 - 10
of 177
pro vyhledávání: '"Katsutoshi Nitta"'
Publikováno v:
The Protein Journal. 25:475-482
In order to investigate the thermodynamics of the unfolding of metalloproteins, the thermal denaturation of bovine alpha-lactalbumin (BLA), a typical calcium-binding protein, was investigated under a wide variety of calcium ion activities by means of
Autor:
Munehito Arai, Masaharu Nakao, Katsutoshi Nitta, Kosuke Maki, Kunihiro Kuwajima, Takumi Koshiba
Publikováno v:
Biochemistry. 44:6685-6692
The intermediate in the equilibrium unfolding of canine milk lysozyme induced by a denaturant is known to be very stable with characteristics of the molten globule state. Furthermore, there are at least two kinetic intermediates during refolding of t
Autor:
Isván Bitter, Tsutomu Yoshida, Tomoyasu Aizawa, Makoto Demura, Katsutoshi Nitta, Klára Tóth, Takatsugu Hirokawa, Yasuhiro Kumaki
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 15:1367-1370
The molecular recognition of neurotransmitters, dopamine and acetylcholine with an amphiphilic resorcinarene receptor was investigated in an aqueous sodium dodecylsulfate (SDS) micelle system by 1H NMR measurements. The interaction distances of these
Publikováno v:
Protein & Peptide Letters. 11:325-330
The effect of pressure on the unfolding of the molten globule (MG) state of canine milk lysozyme (CML) was examined using ultraviolet spectroscopy. The volume changes of the MG-unfolded-state transition were observed at pH 2.0 and around 20 to 60 deg
Publikováno v:
The Protein Journal. 23:335-342
The native and the molten globule states (N and MG states, respectively) of canine milk lysozyme (CML) were examined by CD spectroscopy and AGADIR algorithm, a helix-coil transition program. It revealed that the helical content of the MG state was hi
Publikováno v:
Current Microbiology. 48:383-388
Several properties of chimeric enzymes between a mesophilic isocitrate dehydrogenase (IDH) from a nitrogen-fixing bacterium, Azotobacter vinelandii, and a cold-adapted IDH isozyme (IDH-II) from a psychrophilic bacterium, Colwellia maris, were examine
Autor:
Takashi Kikukawa, Tsunehisa Araiso, Makoto Demura, Kazumi Shimono, Maki Sato, Hirotaka Okita, Katsutoshi Nitta, Naoki Kamo
Publikováno v:
Journal of Biochemistry. 134:151-158
Pharaonis halorhodopsin (phR) is an inward light-driven chloride ion pump in Natronobacterium pharaonis. In order to clarify the roles of the Ser130(phR) and Thr126(phR) residues, which correspond to Ser115(shR) and Thr111(shR) of salinarum hR (shR),
Publikováno v:
Scopus-Elsevier
We have studied the guanidine hydrochloride‒induced equilibrium unfolding and the kinetics of refolding of canine milk lysozyme by circular dichroism and fluorescence spectroscopy. The thermodynamic analysis of the equilibrium unfolding measured by
Autor:
Motoi Kanagawa, Tadayasu Ohkubo, Keiichi Kawano, Shin-Ichiro Nishimura, Shunji Kaya, Kazuya Taniguchi, Katsutoshi Nitta, Tomoyasu Aizawa, Makoto Demura, Naoki Fujitani
Publikováno v:
Biochemical and Biophysical Research Communications. 300:223-229
It has been well established that phosphorylation is an important reaction for the regulation of protein functions. In the N-terminal domain of the alpha-chain of pig gastric H(+)/K(+)-ATPase, reversible sequential phosphorylation occurs at Tyr 10 an
Publikováno v:
Proteins: Structure, Function, and Genetics. 49:472-482
The equilibrium and kinetic folding of hen egg-white lysozyme was studied by means of circular dichroism spectra in the far- and near-ultraviolet (UV) regions at 25 degrees C under the acidic pH conditions. In equilibrium condition at pH 2.2, hen lys