44 research outputs found
Dermatite allergica da contatto all'acido sulfonico fenil benzimidazolico e all'ottil dimetil PABA
No full text
Effect of Ozone Treatment on Suppressivity of a Composted Sewage Sludge on Meloidogyne incognita
No full textInactivation of the reconstituted oxoglutarate carrier from bovine heart mitochondria by pyridoxal 5'-phosphate
No full textThe effect of pyridoxal 5'-phosphate and some other lysine reagents on the purified, reconstituted mitochondrial oxoglutarate transport protein has been investigated. The inhibition of oxoglutarate/oxoglutarate exchange by pyridoxal 5'-phosphate can be reversed by passing the proteoliposomes through a Sephadex column but the reduction of the Schiff's base by sodium borohydride yielded an irreversible inactivation of the oxoglutarate carrier protein. Pyridoxal 5'-phosphate, which caused a time- and concentration-dependent inactivation of oxoglutarate transport with an IC50 of 0.5 mM, competed with the substrate for binding to the oxoglutarate carrier (Ki = 0.4 mM). Kinetic analysis of oxoglutarate transport inhibition by pyridoxal 5'-phosphate indicated that modification of a single amino acid residue/carrier molecule was sufficient for complete inhibition of oxoglutarate transport. After reduction with sodium borohydride [3H]pyridoxal 5'-phosphate bound covalently to the oxoglutarate carrier. Incubation of the proteoliposomes with oxoglutarate or L-malate protected the carrier against inactivation and no radioactivity was found associated with the carrier protein. In contrast, glutarate and substrates of other mitochondrial carrier proteins were unable to protect the carrier. Mersalyl, which is a known sulfhydryl reagent, also failed to protect the oxoglutarate carrier against inhibition by pyridoxal 5'-phosphate. These results indicate that pyridoxal 5'-phosphate interacts with the oxoglutarate carrier at a site(s) (i.e., a lysine residue(s) and/or the amino-terminal glycine residue) which is essential for substrate translocation and may be localized at or near the substrate-binding site.The effect of pyridoxal 5'-phosphate and some other lysine reagents on the purified, reconstituted mitochondrial oxoglutarate transport protein has been investigated. The inhibition of oxoglutarate/oxoglutarate exchange by pyridoxal 5'-phosphate can be reversed by passing the proteoliposomes through a Sephadex column but the reduction of the Schiff's base by sodium borohydride yielded an irreversible inactivation of the oxoglutarate carrier protein. Pyridoxal 5'-phosphate, which caused a time- and concentration-dependent inactivation of oxoglutarate transport with an IC50 Of 0.5 mM, competed with the substrate for binding to the oxoglutarate carrier (K-i = 0.4 mM). Kinetic analysis of oxoglutarate transport inhibition by pyridoxal 5'-phosphate indicated that modification of a single amino acid residue/carrier molecule was sufficient for complete inhibition of oxoglutarate transport. After reduction with sodium borohydride [H-3]pyridoxal 5'-phosphate bound covalently to the oxoglutarate carrier. Incubation of the proteoliposomes with oxoglutarate or L-malate protected the carrier against inactivation and no radioactivity was found associated with the carrier protein. In contrast, glutarate and substrates of other mitochondrial carrier proteins were unable to protect the carrier. Mersalyl, which is a known sulfhydryl reagent, also failed to protect the oxoglutarate carrier against inhibition by pyridoxal 5'-phosphate. These results indicate that pyridoxal 5'-phosphate interacts with the oxoglutarate carrier at a site(s) (i.e., a lysine residue(s) and/or the amino-terminal glycine residue) which is essential for substrate translocation and may be localized at or near the substrate-binding site
Mitochondrial transporters for ornithine and related amino acids: A review
No full textAmong the members of the mitochondrial carrier family, there are transporters that catalyze the translocation of ornithine and related substrates, such as arginine, homoarginine, lysine, histidine, and citrulline, across the inner mitochondrial membrane. The mitochondrial carriers ORC1, ORC2, and SLC25A29 from Homo sapiens, BAC1 and BAC2 from Arabidopsis thaliana, and Ort1p from Saccharomyces cerevisiae have been biochemically characterized by transport assays in liposomes. All of them transport ornithine and amino acids with side chains terminating at least with one amine. There are, however, marked differences in their substrate specificities including their affinity for ornithine (KM values in the mM to μM range). These differences are most likely reflected by minor differences in the substrate binding sites of these carriers. The physiological role of the above-mentioned mitochondrial carriers is to link several metabolic pathways that take place partly in the cytosol and partly in the mitochondrial matrix and to provide basic amino acids for mitochondrial translation. In the liver, human ORC1 catalyzes the citrulline/ornithine exchange across the mitochondrial inner membrane, which is required for the urea cycle. Human ORC1, ORC2, and SLC25A29 are likely to be involved in the biosynthesis and transport of arginine, which can be used as a precursor for the synthesis of NO, agmatine, polyamines, creatine, glutamine, glutamate, and proline, as well as in the degradation of basic amino acids. BAC1 and BAC2 are implicated in some processes similar to those of their human counterparts and in nitrogen and amino acid metabolism linked to stress conditions and the development of plants. Ort1p is involved in the biosynthesis of arginine and polyamines in yeast
A New Batillipedidae (Tardigrada, Heterotardigrada) from the Orosei Gulf, Sardinia, Tyrrhenian Sea
No full textnew species of Batillipedidae, Batillipes spinicauda, has been found in subtidal sand sediments collected in Orosei
Gulf (Sardinia, Tyrrhenian Sea). The most important peculiarities of the new species are the shape of the primary
clavae, lateral processes and caudal apparatus. In the same samples, B. littoralis Renaud-Debyser, 1959 and Orzeliscus
belopus Du Bois-Reymond Marcus, 1952 were found
Substrate specificity of the two mitochondrial ornithine carriers can be swapped by single mutation in substrate binding site
No full textMitochondrial carriers are a large family of proteins that transport specific metabolites across the inner mitochondrial membrane. Sequence and structure analysis has indicated that these transporters have substrate binding sites in a similar location of the central cavity consisting of three major contact points. Here we have characterized mutations of the proposed substrate binding site in the human ornithine carriers ORC1 and ORC2 by carrying out transport assays with a set of different substrates. The different substrate specificities of the two isoforms, which share 87% identical amino acids, were essentially swapped by exchanging a single residue located at position 179 that is arginine in ORC1 and glutamine in ORC2. Altogether the substrate specificity changes demonstrate that Arg-179 and Glu-180 of contact point II bind the Cα carboxylate and amino group of the substrates, respectively. ResidueGlu- 77ofcontactpointImostlikelyinteractswiththeterminal amino group of the substrate side chain. Furthermore, it is likely that all three contact points are involved in the substrate-induced conformational changes required for substrate translocation because Arg-179 is probably connected with Arg-275 of contact point III through Trp-224 by cation-π interactions. Mutations at position 179 also affected the turnover number of the ornithine carrier severely, implying that substrate binding to residue 179 is a rate-limiting step of the catalytic transport cycle. Given that Arg- 179 is located in the vicinity of the matrix gate, it is concluded that it is a key residue in the opening of the carrier to the matrix side. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc
The diversity of Indian Ocean Heterotardigrada
No full textInformation about Indian Ocean tardigrades is quite scarce and in most cases refers to species in coastal coralline sediment and occasionally in abyssal mud. The present data concern species found in the intertidal sand of Coco and La Digue Islands in the Seychelles, previously unsampled for tardigrades, as well as species in subtidal sediment found at depths ranging between 1 and 60 m off the shores of the Maldive Atolls. These sediments are all very similar and consist of heterogeneous coralline sand, moderately or scarcely sorted. Sixteen species (three new to science) were found in the Seychelles, belonging to Renaudarctidae, Stygarctidae, Halechiniscidae, Batillipedidae and Echiniscoididae. Diversity and evenness data are also interesting, with maximum values of H' = 2.59 and of J = 0.97. In the Maldives 25 species were found (two new to science) belonging to Neostygarctidae, Stygarctidae, Halechiniscidae and Batillipedidae. Such a number of species, despite the low percentage of tardigrade fauna (only 0.6% of the total meiofauna), contributes to the high values of both diversity and evenness, with H' ranging between 1.5 and 2.6 and J between 0.6 and 1. The Indian Ocean tardigrade fauna currently numbers 31 species of Arthrotardigrada and 2 species of Echiniscoidida. In the present study, Arthrotardigrada are the most abundant and all the families are present except Neoarctidae. Halechiniscidae is present with all the sub-families (except Euclavartinae), thus contributing to the high diversity values. Furthermore, 18 species, representing more than 50% of the total marine tardigrade fauna, are new records for the Indian Ocean, including five species new to science
