1,552 research outputs found
Analisi di un processo per il riciclo delle acque nell'industria della nobilitazione tessile
No full text
A two stage Spouted Bed Process for Autothermal Pyrolysis or Retorting
No full textFUEL PROCESS TECHNOLOG
Recent structure-activity studies of the peptide hormone urotensin-II, a potent vasoconstrictor
No full textRhynchocyon udzungwensis Rathbun & Rovero 2008
No full text5. Gray-faced Sengi Rhynchocyon udzungwensis French: Sengi a face grise / German: Graugesicht-Risselhlindchen / Spanish: Sengi de cara gris Other common names: Gray-faced Elephant-shrew, Grey-faced Sengi, Grey-faced Elephant-shrew Taxonomy. Rhynchocyon udzungwensis Rathbun & Rovero, 2008, “ Vikongwa River Valley, Ndundulu Forest, West Kilombero Scarp Forest Reserve, Udzungwa Mountains, Iringa Region, Tanzania [7°48.269’S, 36°30.355’E (Arc 1960 datum) |, at 1350 m a.s.l.” This species is monotypic. Distribution. Udzungwa Mts of Eastern Arc Mts, C Tanzania. Descriptive notes. Head-body 297-318 mm, tail 239-262 mm, ear wy mm, hindfoot 79-88 mm; weight 658-750 g. There is no evidence of sexual dimorphism in body size. Tail of the Gray-faced Sengi is ¢.80% of head-body length and is proximally thick and distally tapered. Tail skin is black on dorsal side and dark brown below, with subterminal white, 4-6cm band; tail hair is short, sparse, and same color as skin. Pinnae are nearly hairless, with black to dark brown skin. Hairs on top and sides of face have black bases and cream or white tips giving face a gray appearance, which is diagnostic. Hair behind ears and on shoulders is rufous-yellow, transitions to rufous on dorsum and orange-rufous on sides and becomes black near rump. Hair on venter is pale yellow to cream. Skin on snoutis black and nearly hairless. Snout is exceptionally long and flexible. Dental formulais10-1/3,C1/1,P 4/4, M 2/2 (x2) = 34-36. Upper canines are relatively large, and males have longer upper canines than females. Although not yet reported, presence of diminutive upper incisor presumably is probably variable. Palatal foramina are absent. Postorbital processes are present. Females have two posterior, two intermediate, and no anterior nipples; males have no nipples. Four digits are present on each manus and pes; pollex and hallux are absent. Fifth manual digit is relatively short and has only two phalanges. Post-anal gland is well developed, and pectoral gland is absent. Karyotype is unknown. Habitat. Montane forests (closed canopies and dense leaflitter always present) at elevations of 1000-2300 m. In the northern Mwanihana Forest, some Gray-faced Sengis occur in deciduous to semi-deciduous lowland habitat, which might be suboptimal. Food and Feeding. Diet of the Gray-faced Sengi is probably strictly composed of invertebrates and mostly arthropods, based on similar habitats and shared biology with other species of Rhynchocyon. Breeding. There is no information available for this species, but the Gray-faced Sengi is probably similar to the Black-and-rufous Sengi (R. petersi). Activity patterns. Gray-faced Sengis are fully terrestrial and exclusively diurnal. Nesting is probably similar to that of other species of Rhynchocyon. Each member of a male—female pair probably spends most ofits time independently. Movements, Home range and Social organization. There is no information available for this species, but the Gray-faced Sengi is probably similar to other species of Rhynchocyon. Status and Conservation. Classified as Vulnerable on The IUCN Red List. The Grayfaced Sengi occurs only in Ndundulu-Luhomero and Mwanihana forests, which are prone to stochastic drought-driven and human-induced fires. Its area of occupancy is estimated to be only 390 km?, and its population trend is unknown. Bibliography. Carlen et al. (2017), Corbet & Hanks (1968), Dollman (1912), Evans (1942), Lawson et al. (2013), Olbricht & Stanley (2009), Rathbun (2009, 2013c), Rovero & Rathbun (2015), Rovero et al. (2008).Published as part of Russell A. Mittermeier & Don E. Wilson, 2018, Macroscelididae, pp. 206-234 in Handbook of the Mammals of the World – Volume 8 Insectivores, Sloths and Colugos, Barcelona :Lynx Edicions on page 228, DOI: 10.5281/zenodo.664656
Autoantibodies directed against ribosomal P proteins: use of a multiple antigen peptide as the coating agent in ELISA.
No full textAutoantibodies directed against the ribosomal proteins P0, P1 and P2 (P proteins) are specific for systemic lupus erythematosus (SLE) and there are some evidences that they could be related to the neuropsychiatric manifestations of the disease. In this study, a multiple antigen peptide (MAP) carrying four copies of the C-terminal peptide (13 residues) of the P2 protein, which is a common epitope of the three P proteins, was prepared for use in an ELISA assay. It was employed to detect antibodies directed against the ribosomal P proteins in 102 SLE patients and the results were compared with those obtained using immunoblotting (IB). With this new ELISA, antiribosomal P protein antibodies were found in 15/102 SLE sera. These results correlated well with the results of IB. Furthermore, we confirmed that naturally occurring antiribosomal P protein antibodies are directed mainly against the epitope containing the C-terminal sequence and shared by the three P proteins. MAP appears to be an excellent coating agent for ELISA assays designed to detect anti-P antibodies. Further experiments showed the superiority of MAP, compared to the free peptide, in the detection of weakly positive sera. This ELISA can also be used for the serological follow-up of SLE patients
Unraveling the active conformation of urotensin II
No full textUrotensin II (U-II) is a disulfide-bridged undecapeptide recently identified as the ligand of an orphan G-protein-coupled receptor. Human U-II (H-Glu-Thr-Pro-Asp-cyclo[Cys-Phe-Trp-Lys-Tyr-Cys]-Val-OH) has been described as the most potent vasoconstrictor compound identified to date. With the aim of elucidating the active conformation of hU-II, we have performed a spectroscopic analysis of hU-II minimal active fragment hU-II(4 - 11) in different environmental conditions. The analysis indicated that hU-II(4-11) was highly structured in the anisotropic membrane mimetic SDS solution, showing a type II' beta-turn structure, which is almost unprecedented for L-amino acid peptides. Micelle bound structure of hU-II(4-11) was then compared with those of four synthetic analogues recently synthesized in our lab, bearing modified Cys residues at position 5 and/or position 10 and characterized by different levels of agonist activity. The structures of the active compounds were found to be very similar to that of hU-II(4-11), while a barely active compound does not show any propensity to U-turn formation. Furthermore, distances among putative pharmacophoric points in the structures of the active compounds obtained in SDS solution are in good agreement with those found in a recently described non-peptide agonist of the hU-II receptor. A type II' beta-turn structure was already found for the somatostatin analogue octreotide. On the basis of the similarity of the primary and 3D structures of U-II and somatostatin analogues and on the basis of the sequence homology between the GPR14/UT-II receptor and members of the somatostatin receptor family, a common evolutionary pathway for the signal transmission system activated by these peptide can be hypothesized
Habitat complexity and its use correlate with soil-transmitted helminthiasis in two social groups of Macaca maura (H.R. Schinz, 1825), endangered primates endemic to Sulawesi island, Indonesia
No full textSulawesi endemic Macaca maura is included in the IUCN Red List as Endangered due to
anthropogenic disturbance and fragmentation of its habitat. Residual populations have a scattered
distribution in the karst forests of south Sulawesi. Here the dissolution of limestone layers
has created a multi-level landscape hardly accessible for ground predators and humans. In this
study, we aimed to obtain better knowledge on the ecological flexibility of M. maura in the use
of such a complex habitat, and its consequences on health status. Since all data published on M.
maura were obtained from a single group (group B), an additional group (G) was habituated to
human presence. We analysed 50 vegetation plots (10 × 20 metres) to discriminate structural
features in terms of feeding options (e.g. key food species diversity, density and DBH) and anthropogenic
disturbance (e.g. human trails and solid litter). We then correlated these data with
habitat use and helminth infection. We collected 74 faecal samples from 18 different adult individuals
belonging to both groups. Vegetation analysis suggested that there were 2 suitable habitats:
a Ground Forest (e.g. higher abundance of key food species) and a Karst Tower Forest (e.g.
lower presence of human trails and solid litter). Gastrointestinal investigation revealed a positive
correlation between the prevalence of Trichuris sp. and time devoted to ground food-related activities
in all individuals (Spearman correlation, rs = 0.665, p = 0.003). Moreover, behavioural
data confirmed that group B, the larger study group of the area, spent most of its activity time in
the Ground Forest (N group B = 33 ± 1; N group G = 18 ± 1; χ 2
= 134.30, d.f. = 1, p < 0.001). Since resource
availability and predation risk can influence foraging decisions and, ultimately, space use,
the “group size effect” might explain the significantly higher proportion of time spent by group
B in the Ground Forest. Consequently, due to the Trichuris faecal-oral contamination life-cycle,
the chance of infecting individuals based on their feeding habits might be described according to
the “soil-transmitted helminthiasis hypothesis
Antibodies generated in cats by a lipopeptide reproducing the membrane-proximal external region of the feline immunodeficiency virus transmembrane enhance virus infectivity.
No full textThe immunogenicity of a lipoylated peptide (lipo-P59) reproducing the membrane-proximal external region (MPER) of the transmembrane glycoprotein of feline immunodeficiency virus (FIV) was investigated with cats. In the attempt to mimic the context in which MPER is located within intact virions, lipo-P59 was administered in association with membrane-like micelles. Analyses showed that in this milieu, lipo-P59 had a remarkable propensity to be positioned at the membrane interface, displayed a large number of ordered structures folded in turn helices, and was as active as lipo-P59 alone at inhibiting FIV infectivity in vitro. The antibodies developed differed from the ones previously obtained by immunizing cats with the nonlipoylated version of the peptide (G. Freer, S. Giannecchini, A. Tissot, M. F. Bachmann, P. Rovero, P. F. Serres, and M. Bendinelli, Virology 322:360-369,2004) in epitope specificity and in the fact that they bound FIV virions. However, they too lacked virus-neutralizing activity and actually enhanced FIN infectivity for lymphoid cell cultures. It is concluded that the use of MPER-reproducing oligopeptides is not a viable approach for vaccinating against FIV
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