Fifty-four cases of glucose 6-phosphate dehydrogenase (G6PD) deficiency have so far been reported in Japan. Among them, 21 G6PD variants have been characterized. Nineteen out of the 21 variants were characterized in our laboratory and G6PD Heian and “Kyoto” by others. G6PD Tokyo, Tokushima, Ogikubo, Kurume, Fukushima, Yokohama, Yamaguchi, Wakayama, Akita, Heian and “Kyoto” were classified as Class 1, because all these cases showed chronic hemolytic anemia and severe enzyme deficiency. All these variants showed thermal instability. G6PD Mediterranean-like, Ogori, Gifu and Fukuoka were classified as Class 2, whereas G6PD Hofu, B(-) Chinese, Ube, Konan, Kamiube and Kiwa belonged to Class 3. All the 6 Class 3 variants were found as the results of the screening tests. The incidence of the deficiency in Japanese seems to be 0.1–0.5% but that of the cases which may show drug-induced hemolysis would be much less. G6PD Ube and Konan appear to be relatively common in Japan.
Abstract The γ chain compositions of the fetal hemoglobins of 2453 newborn babies from East Asian countries (1350 babies), from Italy, Yugoslavia, Bulgaria, and Georgia (417 Caucasian babies), and 686 black babies from Georgia were determined by high pressure liquid chromatography. Unusual results for a limited number of babies were confirmed by chemical analyses, and were evaluated further by family studies. Statistical analyses indicated high gene frequencies for the A γ T chain in Italian (f = 0.237), Yugoslavian and Bulgarian (f = 0.238), and white Georgia babies (f = 0.224), a lower frequency in Japan (f = 0.178), and India (f = 0.173), and particularly in mainland China (f = 0.079). The A γ T gene frequency in normal (AA) Black babies was 0.102. When a β S or β C mutation was also present this frequency was greatly decreased, particularly in babies with the AC condition (f = 0.036). These results suggest the near absence of the A γ T mutation on the chromosome also carrying the β C determinant. Most babies had the expected G γ values which vary between 60 and 80%, but several (mainly black) babies had higher values (between 80 and 90%), while one normal black baby had a G γ value of (nearly) 100%. This condition may be a form of A γ +1 ‐thalassemia and has been discussed in detail elsewhere (Blood 58:491‐500, 1981). Thirty‐five clinically normal (mainly Chinese, Indian, and Japanese) babies had G γ values of about 40%. Twenty‐six babies had A γ 1 values of about 60%, while the remaining nine babies had A γ T and A γ I chains in a ratio of either 1 to 2 or 1 to 1. Two additional newborns did not produce any G γ chains, but had only A γ I chains or A γ I chains. Family studies failed to indicate a specific hematological abnormality. These unusual ratios between the G γ and (either A γ I or A γ T ) chains have led to speculations regarding possible genetic abnormalities present in these infants.
Abstract The oxidized form of glutathione transport was studied in human erythrocytes in pyrimidine 5′‐nucleotidase (P5N) deficiency, a disorder in which the amounts of CTP and UTP in the erythrocytes are elevated. The inhibition of ATP‐requiring oxidized glutathione (GSSG) transport by CTP and UTP is believed to play a role in elevating the levels of the reduced form of glutathione (GSH) in the erythrocytes of patients with P5N deficiency. The current investigation was undertaken to determine if GSSG transport actually decreases in the erythrocytes of such patients. Erythrocytes from a 17‐year‐old patient and a 13‐year‐old patient with P5N deficiency hemolytic anemia and from ten normal subjects were used as materials for the experiment. Erythrocytes, which had been previously incubated with [ 3 H]glycine, were incubated at 37°C, and the rate of [ 3 H]GSSG transported by the cells was estimated. The velocity of GSSG transport out of the erythrocytes was quite low in the patients, 3.17–3.65 nmol GSSG/ml erythrocytes/hr at 37°C in one case, and 3.30 nmol GSSG/ml erythrocytes/hr in the other case, vs that in the normal controls (6.00 ± 0.80 nmol GSSG/ml erythrocytes/hr; mean ± SD). The activity of γ‐glutamylcysteine synthetase and glutathione synthetase did not decrease in the patients. Decreased transport activity of GSSG in addition to a normal synthesis rate for GSH may explain the increased concentration of erythrocyte GSH in P5N deficiency.
We investigated the genetic basis for the increased adenosine deaminase (ADA) expression in adult T-cell leukemia (ATL). We found a correlation between the levels of ADA-specific mRNA and ADA immunoreactive protein in ATL. Southern blot analysis revealed no gene amplification or rearrangement of the ADA gene. These findings indicate that increased ADA expression in ATL cells reflects increased transcriptional activity for the ADA gene or increased stability of ADA mRNA.
When exposed to a high-temperature oxidizing environment, Rh catalysts supported on Al2O3-based oxides lose their three-way catalytic activity as a result of unfavorable interface interactions that allow Rh3+ to diffuse into the support structure and occupy Al3+ sites. This study showed that the incorporated Rh3+ ions were not easily reduced to active Rh metal species and caused substantial thermal deactivation. The deactivation was most obvious for γ-Al2O3 and MgAl2O4 with a spinel-type structure but much less for hexaaluminate (LaMgAl11O19) with a layered structure consisting of alternative stacking of a spinel block and a La–O monolayer. After annealing at 900 and 1000 °C for 100 h in the air, Rh-deposited single crystals were studied by dynamic secondary ion mass spectrometry to analyze the Rh depth profile. The Rh depth profile in LaMgAl11O19 showed that the diffusion along the c axis (∥c) was significantly suppressed compared to that normal to the c axis (⊥c). The diffusion of Rh3+ was faster and nearly isotropic in a MgAl2O4 single crystal, which was used as a model crystal for γ-Al2O3. These results show that the layered structure of hexaaluminate influences the Rh3+ diffusion, i.e., the La–O interlayer between closely packed spinel blocks running at every approximately 1.1 nm interval is likely the diffusion barrier. This barrier effectively blocks further penetration of the incorporated Rh3+ ions from the surface and preserves their smooth reduction to active metallic Rh nanoparticles.
