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Abstract: Some of 1,6-(N-substituted) aza-[60] fulleroids (1) and their corresponding photochemical reaction products, 1,2-(N-substituted) aziridino-[60] fullerenes (2) showed peculiar transient absorption peaks depending on the N-substituents. Although these bands are considered to concern with very slow photochemical rearrangements 1 → 2 in the excited triplet state, no definitive evidence has been obtained yet. We report on the character of the excited triplet states in these compounds by means of a time-resolved electron paramagnetic resonance technique. Definitive evidence on the involvement of intra-molecular charge transfer states is shown in this Letter. [Copyright &y& Elsevier]

Time-resolved EPR spectra were observed by means of the transient EPR technique for two kinds of fullerene dimers C120 and C120O in the lowest excited triplet (T1) states and compared with those of mono-adducts of fullerene (C60). It was found that zero-field splitting (zfs) parameters of both dimers are nearly the same as those of the monomers, indicating that the excitation is almost completely localized at one of the two fullerene units in the T1 state. [Copyright &y& Elsevier]

Anti-insulin immunoglobulin G (IgG) has been found in the sera of healthy cats. To determine the concentrations of these antibodies, an enzyme-linked immunosorbent assay (ELISA) for anti-insulin IgG was developed. ELISA maintained the linearity of a standard concentration line between 67.5 and 2160 ng/ml. The coefficients of variances (CVs) of intra-assays in two different plasma samples were 4.0% and 3.7%, respectively. The inter-assay CVs in two different plasma samples were 5.1% and 6.9%, respectively. The dilution curves of two samples were rectilinear. Anti-insulin IgG was detected in all 84 of the healthy cats that were tested. Plasma anti-insulin IgG concentrations ranged from 80 to 1578 μg/ml, with a median concentration of 221 μg/ml, and this value correlated positively with total plasma IgG concentrations (r = 0.383, p < 0.01). In an intravenous glucose tolerance test, plasma antiinsulin IgG concentrations did not alter, even with changes in plasma glucose and insulin concentrations. The ELISA that was developed was able to determine plasma anti-insulin IgG in domestic cats, and confirmed that all healthy cats had plasma anti-insulin IgG. Determining the plasma concentrations of antiinsulin IgG in cats with various pathological conditions might clarify the role of anti-insulin IgG. [ABSTRACT FROM AUTHOR]

Abstract: In alkaline aqueous solutions, 3,4-diaminobenzoate (H2(2LPDA)−) reacts with PtII to form a 1:2 (Pt:L) complex that intensely absorbs near-infrared (NIR) light at 713nm (ε =8.0×104 M−1 cm−1). The absorption disappeared at pH<3 (in DMSO), showing pH-responsive switching of the NIR absorption. By comparing the NIR-absorbing behavior of this complex to that of a complex, [PtII(1LISQ)2]2−, containing the analogous phenylenediamine ligand [(1LISQ)2− = o-diiminobenzosemiquinonate radical], the complex can be formulated as [PtII(2LISQ)2]2−. The assignment of the entity was consistent with the redox and spectroelectrochemical behaviors and electronic spin resonance (ESR) spectroscopy. First, one-electron oxidation of [PtII(2LISQ)2]2− formed an ESR-silent complex assignable to the dimeric complex [{PtII(2LISQ)(2LIBQ)}2]2− [(2LIBQ)= o-iminobenzoquinone form] in which the two radical centers at were antiferromagnetically coupled. Second, the one-electron reduced complex of [PtII(2LISQ)2]2− exhibited an ESR signal attributed to [PtII(2LISQ)(2LPDA)]3− ; 34% of the electronic spin was located at the PtII center rather than on the moiety. The pH-responsive switching-off of the NIR absorption was thus rationally explained by oxidation of [PtII(2LISQ)2]2− to [{PtII(2LISQ)(2LIBQ)}2]2− by the increase of the rest potential of the solution in the lower pH region. [Copyright &y& Elsevier]

Abstract: Peroxisome proliferator-activated receptors (PPARs) are ligand-activated transcription factors implicated in lipid metabolism. In this study, the full-length cDNA of canine PPARβ and γ were sequenced, and expression of PPARs was evaluated in normal tissues and primary cultures of adipocytes in dogs, followed by investigations for polymorphisms of canine PPARγ. Comparison of the deduced amino acid sequences of canine PPARβ and γ cDNA with that of human PPARβ and γ cDNA revealed 95.9% and 98.2% identity, respectively. PPARβ expression was ubiquitous and high PPARγ expression was detected in the subcutaneous and omental adipose tissues, spleen and large intestine. Canine PPARγ mRNA expression in cultured adipocytes began to increase from 4 days after induction of differentiation, and increased nearly ninefold within 10 days after induction of differentiation. Although expression level of PPARα was low in the cultured adipocytes, it slightly increased within 10 days. In contrast, expression of PPARβ showed only small variations during adipocyte differentiation, though expression levels were relatively high. These results suggest that PPARγ may play an important role in adipocyte differentiation in dogs. Investigations for polymorphisms of PPARγ revealed a silent polymorphism, C1362T, in 3 of 92 dogs. [Copyright &y& Elsevier]