A generic morphological model of the anatomic variability in the m. flexor digitorum profundus, m. flexor pollicis longus and mm. lumbricales complex

This study examined the productivity and representation of past-tense marking in children with and without specific language impairment (SLI). Participants were 11 6-year-olds with SLI, 11 age-matched controls, and 11 MLU-matched controls. Regular and irregular verbs were used to examine the productivity of regular marking. Past-tense representation was examined by asking children to inflect homophonous pairs of denominal and irregular root verbs. All three groups demonstrated productive marking of past tense, although as expected the accuracy of the impaired groups was less than that of earlier control group. Patterns of past-tense marking as a function of a word's phonological composition and inflectional frequency were the same for the SLI- and MLU-matched groups, and all children presented a past-tense system that was sensitive to grammatical structure. The findings replicate previous research of the SLI morphological system and provide additional specification of these children's morphological strengths and weaknesses. Strengths include the children's sensitivity to grammatical and phonological characteristics of the lexicon; weaknesses include limited productivity of regular past-tense marking and a greater sensitivity to frequency manipulations as compared to normally developing children. Results are discussed in terms of the nature of the SLI profile. They also are used to evaluate the theoretical model on which the study was based.     

IN VITRO ANTIOXIDANT AND ANTICANCER ACTIVITIES OF EXTRACTS FROM A FERMENTED FOOD

Solvent extracts were prepared from Manda Enzyme®, one of the fermented health foods, and their activities of radical scavenging and cancer cell growth inhibition were evaluated. Manda Enzyme® was extracted with 55% ethanol, and then fractionated into n‐hexane, chloroform, ethyl acetate, methanol‐soluble and methanol‐insoluble fractions. The antioxidant activities were in the order chloroform > ethyl acetate > other fractions and of each fraction were positively related to the amount of total phenolics and the intensity of brown color. The cancer cell growth inhibitory activities were in the order n‐hexane > chloroform > other fractions. Proliferation of HRT‐18, HCT‐48 and HepG2 human cancer cells was inhibited by the treatment of the n‐hexane fraction of Manda Enzyme® at a concentration of 400 μg/mL to the extent of 75, 89 and 90%, respectively. From these results, it is considered that Manda Enzyme® has chemically different ingredients showing strong antioxidant and anticancer activity in vitro.     

Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: a novel multihemic cytochrome bc, a new complex III

Rhodothermus marinus, a thermohalophilic bacterium, has a unique electron-transfer chain, containing, besides a cbb3 and a caa3 terminal oxidases, a novel cytochrome bc complex [Pereira, M. M., Carita, J. N., and Teixeira, M. (1999) Biochemistry 38, 1268-1275]. The membrane-bound iron-sulfur centers of this bacterium were studied by electron paramagnetic resonance (EPR) spectroscopy, leading to the identification of its main electron-transfer complexes. The resonances typical for the Rieske-type centers are not detected. Clusters S1 and S3 from succinate dehydrogenase were identified; interestingly, center S3 is shown to be present in two different conformations, with g values at 2.035, 2.009, and 2.001 and at 2.025, 2.002, and 2.000. Upon addition of NADH and dithionite, EPR signals assigned to resonances characteristic of binuclear and tetranuclear clusters develop and are attributed to the iron-sulfur centers of complexes I and II. A high-potential iron-sulfur protein- (HiPIP-) type center previously detected in the membranes of this bacterium [Pereira et al. (1994) FEBS Lett. 352, 327-330] is shown to belong indeed to a canonical HiPIP. This protein was purified and extensively characterized. It is a small water-soluble protein of approximately 10 kDa, containing a single [4Fe-4S]3+/2+ cluster. The reduction potential, determined by EPR redox titrations in intact and detergent-solubilized membranes as well as by cyclic voltammetry in solution, has a pH-independent value of 260 +/- 20 mV, in the range 6-9. In vitro reconstitution of the R. marinus electron-transfer chain shows that the HiPIP plays a fundamental role in the chain, as the electron shuttle between R. marinus cytochrome bc complex and the caa3 terminal oxidase, being thus simultaneously identified a HiPIP reductase and a HiPIP oxidase.