Zobrazeno 1 - 10
of 124
pro vyhledávání: '"Kozo Hamaguchi"'
Autor:
Yasushi Kawata, Kozo Hamaguchi
Publikováno v:
Protein Science. 4:416-420
The stability of ribonuclease T2 (RNase T2) from Aspergillus oryzae against guanidine hydrochloride and heat was studied by using CD and fluorescence. RNase T2 unfolded and refolded reversibly concomitant with activity, but the unfolding and refoldin
Autor:
Yasushi Kawata, Kozo Hamaguchi
Publikováno v:
Biochemistry. 30:4367-4373
The CL fragment of a type-kappa immunoglobulin light chain in which the C-terminal cysteine residue was modified with N-(iodoacetyl)-N'-(5-sulfo-1-naphthyl)ethylenediamine (CL-AEDANS fragment) was prepared. This fragment has only one tryptophan resid
Publikováno v:
Biochemistry. 29:4424-4429
In spite of its short polypeptide chain, the pancreatic polypeptide molecule consists of a polyproline I1 type helix and a-helix. To understand the stability and formation of the a-helical region, we prepared some peptide fragments including the heli
Autor:
Yasushi Kawata, Kozo Hamaguchi
Publikováno v:
Biopolymers. 30:389-394
Hydrogen-exchange rates of the indole NH proton of a tryptophan residue, buried fully in the interior of each of the constant (CL) and variable (VL) fragments of a type-kappa-immunoglobulin light chain, were studied at various pH values and at 25 deg
Publikováno v:
Biochemistry. 30(31)
Constant fragments with different carboxyl terminals, CL(109-211), CL(109-207), and CL-(109-200), were prepared by limited carboxypeptidase P or Y proteolysis of the constant fragment, CL-(109-214), of a type lambda immunoglobulin light chain, and th
Publikováno v:
Biochemistry. 29(39)
The role of tryptophan residues in the stability of proteins was studied by ozone oxidation, which causes a small change in the tryptophan side chain. Trp 187 of the constant fragment of a type lambda immunoglobulin light chain, Trp 59 of ribonucleas
Autor:
Yasushi Kawata, Kozo Hamaguchi
Publikováno v:
Journal of Protein Chemistry. 11:414-415
Publikováno v:
The Journal of Biochemistry. 77:993-1006
The pH dependence of the extrinsic circular dichroic (CD) band at 375 nm of hen egg-white lysozyme [EC 3.2.1.17] in which Trp 62 had selectively 2-nitrophenylsulfenylated (NPS-lysozyme) was studied. This pH dependence was interpreted in terms of the
Publikováno v:
The Journal of Biochemistry. 91:1777-1788
The chemical reaction of p-bromophenacyl bromide (BPB) with His 48 of cobra venom phospholipases A2 (N. naja siamensis, N. naja kaouthia, and N. naja atra) was studied at 25 degrees C and ionic strength 0.1 by following the decreases in the fluoresce
Publikováno v:
The Journal of Biochemistry. 78:705-711
The difference spectra of hen and turkey egg-white lysozymes [EC 3.2.1.17] produced by acidification were measured. The difference spectra of both lysozymes had peaks at 295 and 301 nm which are characteristic of tryptophyl residues. The pH dependenc