A Clinical Study on Ureterosigmoidostomy and Ureterorectostomy

Hoshino, Yoshinobu; Tomoishi, Junzo; Kunisawa, Y; S, Aoki

doi:10.5980/jpnjurol1928.72.10_1227

Cited by 2 publications

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“…The ternary complexes Cu( l -XPhe)(DA)NO 3 in aqueous solution showed several peaks in the UV region and a d−d absorption peak at 605−613 nm at neutral pH. The difference spectra that were obtained by subtracting the spectra for 1:1:1 Cu(II)−DA− l -alaninate and l -XPhe from the spectrum for Cu( l -XPhe)(phen)NO 3 gave a weak broad peak at 320−400 nm, which is ascribable to the charge transfer (CT) between stacked aromatic rings in the complexes . As shown in Figure , the absorption intensity around 350 nm increased with the increase of the electron donating ability of the para -substituent groups (the difference spectrum for Cu( l -NO 2 Phe)(phen) exhibited a negative peak), the order being NO 2 ≪ H < OH < NH 2 .…”

Section: Resultsmentioning

confidence: 99%

Structural Dependence of Aromatic Ring Stacking and Related Weak Interactions in Ternary Amino Acid−Copper(II) Complexes and Its Biological Implication

et al. 1997

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Structures and stabilization due to stacking of ternary copper(II) complexes containing an aromatic amino acid (AA) and an aromatic diamine (DA), Cu(AA)(DA), have been investigated by potentiometric, spectroscopic, and X-ray diffraction methods. For the systems with AA ) para-X-substituted L-phenylalanine (L-XPhe; X ) H, NO 2 , OH, NH 2 ) and DA ) 2,2′-bipyridine (bpy) or 1,10-phenanthroline (phen), the difference absorption spectra in the region 320-400 nm exhibited a peak assignable to the charge transfer interaction between the aromatic rings of DA and L-XPhe, the intensity being in the order NH 2 > OH > H . NO 2 with respect to X. The stability constants of Cu(AA)(DA) determined for AA ) DL-XPhe (X ) F, Cl, Br) and L-XPhe (X ) NH 2 , NO 2 , I) at 25 °C and I ) 0.1 M (KNO 3 ) indicated that stabilization of Cu(L-XPhe)(DA) relative to Cu(L-Ala)(en) (Ala ) alanine; en 3), and [Cu(L-Phe)-(bpy)]ClO 4 ‚H 2 O (4), isolated as crystals, were determined by the X-ray diffraction method: 1, orthorhombic,All of the complexes have a similar distorted square-pyramidal structure around the central Cu(II) ion. While 1 and 2 have a structure involving aromatic ring stacking in the solid state, 4 has a structure without it and 3 has both types of structures in the unit cell.

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Section: Resultsmentioning

confidence: 99%

Structural Dependence of Aromatic Ring Stacking and Related Weak Interactions in Ternary Amino Acid−Copper(II) Complexes and Its Biological Implication

et al. 1997

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“…It should be mentioned that Yoshino et al (1972) and Yoshino (1976) modified HMM with 2-hydroxy-5-nitrobenzyl bromide, a reagent that is similar to but not identical with DHNBS, and found two HNB bound at a 100-fold molar excess of reagent over HMM. One of the two HNB was bound to the S-2 segment and the other to one of the two S-l segments of the HMM.…”

Section: Discussionmentioning

confidence: 99%

Modification of myosin subfragment 1 tryptophans by dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide

Werber¹,

Peyser²,

Mühlrád³

1987

Biochemistry

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Modification of tryptophanyl residues (Trps) of myosin subfragments 1 (S-1) was performed with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide (DHNBS). Under controlled conditions, pH 6 at 0 degrees C and 10-min reaction with 10-100-fold molar excess, K+(EDTA) activity was reduced down to less than half, whereas Ca2+-ATPase activity increased and acto-S-1-ATPase was not affected. The number of modified Trps (up to 2.5) agreed well with the number of 2-hydroxy-5-nitrobenzyl moieties incorporated in S-1. The thiol groups of S-1 were not affected up to 50-fold molar excess of DHNBS, thus indicating that the modification was selective for Trps. The modification of as few as one Trp caused a blue shift of the emission spectrum, accompanied by a reduction in the fluorescence quantum yield. The accessibility of Trps to the fluorescence quencher acrylamide is drastically reduced upon modification, indicating that DHNBS-reactive Trps are more "exposed" than the DHNBS-refractive ones. DHNBS modification did not seem to affect the ATP-induced tryptophan fluorescence enhancement of S-1. The effect of DHNBS modification of the intrinsic fluorescence of S-1 indicates that the modified Trps are located in a polar environment and that they may be identical with the long-lifetime Trps of Torgerson [Torgerson, P. (1984) Biochemistry 23, 3002-3007]. The most reactive Trp is located in the N-terminal 27-kDa fragment of the S-1 heavy chain. It might also be inferred from the above data that the nonexposed and ATP-perturbed Trp(s) is (are) located in the 50-kDa fragment.

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A Clinical Study on Ureterosigmoidostomy and Ureterorectostomy

Cited by 2 publications

References 0 publications

Structural Dependence of Aromatic Ring Stacking and Related Weak Interactions in Ternary Amino Acid−Copper(II) Complexes and Its Biological Implication

Structural Dependence of Aromatic Ring Stacking and Related Weak Interactions in Ternary Amino Acid−Copper(II) Complexes and Its Biological Implication

Modification of myosin subfragment 1 tryptophans by dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide

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