Threonine-303 of rabbit P450 2E1, which is putatively located at the distal heme surface, was replaced by serine and valine via site-directed mutagenesis. In the oxidized state, the Ser-mutated P450 exhibited a low- and high-spin mixed-type (low > high) absorption spectrum, whereas the Val-mutated P450, like the wild-type P450, exhibited a nearly high-spin type spectrum. The reduced CO complexes of the Ser- and Val-mutated P450s, as well as that of the wild-type P450, showed a Soret absorption maximum at 452 nm. Both mutated P450s were active in the hydroxylation of C10 to C18 fatty acids at somewhat lower rates than the wild-type P450. The Val-mutated P450 gave the same two products (the major one is probably the omega-1 hydroxy analog) as the wild-type P450, while additional products were formed on incubation with C11 to C17 fatty acids as substrates of the Ser-mutated P450; a total of four products was detected for each of the C12 to C15 fatty acids, and three for each of the C11, C16, and C17 homologues. The metabolites of laurate were determined by GC-MS analysis to be the omega-1, omega-2, omega-3, and omega-4 hydroxy counterparts. The Ser-mutated P450 hydroxylated drug substrates at almost the same rates as the wild-type P450, while the mutation to valine significantly lowered the drug hydroxylase activities.(ABSTRACT TRUNCATED AT 250 WORDS)

We have developed a direct fabrication method of oxide TFT on a flexible substrate and a flexible color filter array (CFA) technology for white OLED. The oxide TFT is successfully integrated on the flexible substrate and the fabricated display achieved wide color gamut of NTSC (in CIE u'v' space) more than 100%. Display Size 9.9" Number of Pixels 960  RGBW  540 (qHD) Pixel Size 228 m  228 m Resolution 111 ppi Number of Colors 16,777,216 Operation Scheme 2Tr Thickness 110 m 74.1L / M. Noda Late-News Paper 998 • SID 2012 DIGEST ISSN 0097-966X/12/4302-0998-$1.00

Gamma-aminobutyric acid (GABA) is an inhibitory neurotransmitter with beneficial effects including antihypertension and antistress properties. In this study, we examined the effects of GABA-enriched white rice (GABA rice) on blood pressure (BP) in 39 mildly hypertensive adults in a randomized, double-blind, placebo-controlled study. The participants were divided into a test group (n = 22) who consumed rice with 11.2 mg GABA/100 g of rice and a placebo group (n = 17) who consumed rice with 2.7 mg GABA/100 g of rice. For 8 weeks, the participants took 150 g of either the GABA rice or the placebo rice. Hematological examinations were performed on both groups at 0, 4, and 8 weeks after the start of rice consumption. Home BP was self-measured two times daily, morning and evening, from 1 weeks before to 2 weeks after the intervention. Although the hospital BP and evening BP measurements of the participants showed no significant change, consumption of the GABA rice improved the morning BP compared with the placebo rice after the 1st week and during the 6th and 8th weeks. These results showed the possibility that the GABA rice improves morning hypertension.

P450 2C2 as well as P450 2E1 [Fukuda, T. et al. (1993) J. Biochem. 113, 7-12] catalyzed the hydroxylation of medium chain fatty acids, although the regioselectivity of substrates of the former contrasted with that of the latter. Whereas P450 2E1 hydroxylated C9-C18 fatty acids at the omega-1 position and to a much lesser extent at the omega and omega-2 positions, P450 2C2 hydroxylated C9-C13 fatty acids at different positions dependent on the chain length of fatty acids. Among the fatty acids used as the substrate, undecanoate was hydroxylated at the omega-1 position almost exclusively by P450 2C2. The proportion of omega-hydroxylated products produced by P450 2C2 was markedly increased with decreasing chain length of fatty acids, while the hydroxylation positions were enlarged to the omega-3 position with tridecanoate. When the conserved Thr at the putative distal helix was replaced with Ser, the substrate regioselectivity of the two P450s was affected in different manners. The mutation of P450 2C2 did not change the hydroxylation positions of C9-C12 fatty acids, but caused a significant decrease in the proportion of the omega-1 hydroxy analog in the total products. In sharp contrast to P450 2C2, the mutated P450 2E1 gave additional products to those with the wild-type P450, and the number of different products increased with increasing chain length of the fatty acids. Thus, the products of palmitate hydroxylation were identified as omega-1, omega-2, omega-3, omega-4, omega-5, omega-6, and omega-7 monohydroxy isomers using gas chromatography-electron impact mass spectrometry.(ABSTRACT TRUNCATED AT 250 WORDS)

No abstract