アシダ ヒトシ ノ コクサイ セイジカン 2 カン マンシュウ ジヘン ゼンゴ ニ オケル レンゾクセイ ヲ チュウシン ニ

論

アシダ ヒトシ ノ コクサイ セイジカン 1 マンシュウ ジヘン ゼンゴ ニ オケル レンゾクセイ ヲ チュウシン ニ

論

THE ENHANCEMENT OF THE EFFECT OF B.C.G. VACCINATION WITH HYALURONIDASE

ArticleJournal of the Shinshu University. 4: 39-71(1954)departmental bulletin pape

Epithelioid Sarcoma of the Forearm Arising from Perineural Sheath of Median Nerve Mimicking Carpal Tunnel Syndrome

We report here a case of epithelioid sarcoma in the forearm of a 33-year-old male presenting with symptoms and signs of carpal tunnel syndrome originating from the direct involvement of the median nerve. Due to the slow growing of the tumor, the patient noticed the presence of tumor mass in his forearm after several months from the initial onset of the symptoms. Magnetic resonance imaging showed an 8 × 4 cm mass involving the median nerve in the middle part of the forearm, and histological analysis of the biopsy specimen revealed the diagnosis of epithelioid sarcoma. Radical surgical resection was performed in conjunction with adjuvant chemotherapy. The function of the flexors were restored by the multiple tendon transfers (EIP → FDS; ECRL → FDP; BrR → FPL; EDM → opponens) with superficial cutaneous branch of radial nerve transfer to the resected median nerve. The function of the affected hand showed excellent with the DASH disability/symptom score of 22.5, and both the grasp power and sensory of the median nerve area has recovered up to 50% of the normal side. The patient returned to his original vocation and alive with continuous disease free at 3.5-year follow-up since initial treatment

Structural phase diagram of LaO1-xFxBiSSe: suppression of the structural phase transition by partial F substitutions

We have investigated low-temperature crystal structure of BiCh2-based compounds LaO1-xFxBiSSe (x = 0, 0.01, 0.02, 0.03, and 0.5), in which anomalous two-fold-symmetric in-plane anisotropy of superconducting states has been observed for x = 0.5. From synchrotron X-ray diffraction experiments, a structural transition from tetragonal to monoclinic was observed for x = 0 and 0.01 at 340 and 240 K, respectively. For x = 0.03, a structural transition and broadening of the diffraction peak were not observed down to 100 K. These facts suggest that the structural transition could be suppressed by 3% F substitution in LaO1-xFxBiSSe. Furthermore, the crystal structure for x = 0.5 at 4 K was examined by low-temperature (laboratory) X-ray diffraction, which confirmed that the tetragonal structure is maintained at 4 K for x = 0.5. Our results suggest that the two-fold-symmetric in-plane anisotropy of superconducting states observed for LaO0.5F0.5BiSSe was not originated from structural symmetry lowering.Comment: 15 pages, 5 figures + 3 supplemental figure

Structural basis of L-glucose oxidation by scyllo-inositol dehydrogenase: Implications for a novel enzyme subfamily classification

For about 70 years, L-glucose had been considered non-metabolizable by either mammalian or bacterial cells. Recently, however, an L-glucose catabolic pathway has been discovered in Paracoccus laeviglucosivorans, and the genes responsible cloned. Scyllo-inositol dehydrogenase is involved in the first step in the pathway that oxidizes L-glucose to produce L-glucono-1,5-lactone with concomitant reduction of NAD+ dependent manner. Here, we report the crystal structure of the ternary complex of scyllo-inositol dehydrogenase with NAD+ and L-glucono-1,5-lactone at 1.8 Å resolution. The enzyme adopts a homo-tetrameric structure, similar to those of the inositol dehydrogenase family, and the electron densities of the bound sugar was clearly observed, allowing identification of the residues responsible for interaction with the substrate in the catalytic site. In addition to the conserved catalytic residues (Lys106, Asp191, and His195), another residue, His318, located in the loop region of the adjacent subunit, is involved in substrate recognition. Site-directed mutagenesis confirmed the role of these residues in catalytic activity. We also report the complex structures of the enzyme with myo-inositol and scyllo-inosose. The Arg178 residue located in the flexible loop at the entrance of the catalytic site is also involved in substrate recognition, and plays an important role in accepting both L-glucose and inositols as substrates. On the basis of these structural features, which have not been identified in the known inositol dehydrogenases, and a phylogenetic analysis of IDH family enzymes, we suggest a novel subfamily of the GFO/IDH/MocA family. Since many enzymes in this family have not biochemically characterized, our results could promote to find their activities with various substrates

Structural basis for the substrate recognition of aminoglycoside 7′′-phosphotransferase-Ia from Streptomyces hygroscopicus

Hygromycin B (HygB) is one of the aminoglycoside antibiotics, and it is widely used as a reagent in molecular-biology experiments. Two kinases are known to inactivate HygB through phosphorylation: aminoglycoside 7′′-phosphotransferase-Ia [APH(7′′)-Ia] from Streptomyces hygroscopicus and aminoglycoside 4-phosphotransferase-Ia [APH(4)-Ia] from Escherichia coli. They phosphorylate the hydroxyl groups at positions 7′′ and 4 of the HygB molecule, respectively. Previously, the crystal structure of APH(4)-Ia was reported as a ternary complex with HygB and 5′-adenylyl-β,γ-imidodiphosphate (AMP-PNP). To investigate the differences in the substrate-recognition mechanism between APH(7′′)-Ia and APH(4)-Ia, the crystal structure of APH(7′′)-Ia complexed with HygB is reported. The overall structure of APH(7′′)-Ia is similar to those of other aminoglycoside phosphotransferases, including APH(4)-Ia, and consists of an N-terminal lobe (N-lobe) and a C-terminal lobe (C-lobe). The latter also comprises a core and a helical domain. Accordingly, the APH(7′′)-Ia and APH(4)-Ia structures fit globally when the structures are superposed at three catalytically important conserved residues, His, Asp and Asn, in the Brenner motif, which is conserved in aminoglycoside phosphotransferases as well as in eukaryotic protein kinases. On the other hand, the phosphorylated hydroxyl groups of HygB in both structures come close to the Asp residue, and the HygB molecules in each structure lie in opposite directions. These molecules were held by the helical domain in the C-lobe, which exhibited structural differences between the two kinases. Furthermore, based on the crystal structures of APH(7′′)-Ia and APH(4)-Ia, some mutated residues in their thermostable mutants reported previously were located at the same positions in the two enzymes

Magnetostriction studies up to megagauss fields using fiber Bragg grating technique

We here report magnetostriction measurements under pulsed megagauss fields using a high-speed 100 MHz strain monitoring system devised using fiber Bragg grating (FBG) technique with optical filter method. The optical filter method is a detection scheme of the strain of FBG, where the changing Bragg wavelength of the FBG reflection is converted to the intensity of reflected light to enable the 100 MHz measurement. In order to show the usefulness and reliability of the method, we report the measurements for solid oxygen, spin-controlled crystal, and volborthite, a deformed Kagom\'{e} quantum spin lattice, using static magnetic fields up to 7 T and non-destructive millisecond pulse magnets up to 50 T. Then, we show the application of the method for the magnetostriction measurements of CaV$_{4}$O$_{9}$, a two-dimensional antiferromagnet with spin-halves, and LaCoO$_{3}$, an anomalous spin-crossover oxide, in the megagauss fields.Comment: 9pages, 6 figures, Conference proceedings for MegaGauss16 at Kashiwa, Japan in Sept. 201