Characterization of a wine-like beverage obtained from sugarcane juice

Two yeasts (Saccharomyces cerevisiae and Saccharomyces cerevisiae var ellipsoideus)were tested for their ability to ferment sugarcane (Saccharum officinarum) juice. In order to do this, time course studies of volatile, fixed, and total acidity, pH, alcohol, total sugars and °Bx were performed and the presence of methanol was tested. The fermentation studies were carried out at 25, 28 and 30 °C and the juice was inoculated with 1 and 5% (v/v) suspensions of both yeasts containing 1 × 10⁸ cells ml⁻¹. Time course studies indicated a similar fermentative pattern at the three temperatures evaluated, hence 25 °C was chosen as the cheapest alternative. The size of the inoculum made no difference in the fermentation. Analyses of the sugarcane juice wine showed the following results: pH, 3.2; alcohol, 10 °GL; total solids, 16.5 g l⁻¹; ash, 1.4 g l⁻¹; total acidity, 5.4 g l⁻¹; volatile acidity, 0.12 g l⁻¹; fixed acidity, 5.3 g l⁻¹ and no methanol was detected. Two additional products were obtained after adding passion fruit juice and roselle (Hibiscus sabdarifa Linn) concentrates. The fruit-flavoured wines were significantly preferred (P ≤ 0.05) over the plain product. These results indicated that the elaboration of wine-like beverages is a good alternative use for sugarcane.     

Array assessment of phage-displayed peptide mimics of Human Immunodeficiency Virus type 1 gp41 immunodominant epitope: binding to antibodies of infected individuals

An array of phage-displayed mimetic peptides representing 18 sequences from the HIV-1 gp41 immunodominant epitope was fabricated on a nitrocellulose membrane. It used to compare the antibody-binding affinity of the peptide and to monitor the immune response of four patients prior to and after the initiation of Highly Active Anti-Retroviral Therapy in parallel assays with several probes using near-infrared fluorescence detection. The proposed multiplexed approach is highly sensitive, consumes less sample and can be used to analyze the immune repertoires of virus-infected individuals.     

Guías clínicas de fractura de cadera. Comparación de sus principales recomendaciones

Hip fracture is the most severe complication of osteoporosis, and despite being a frequent health problem, there is a wide variability in both the health care provided to these patients and the results achieved after their treatment. Clinical guidelines are a tool that helps to reduce this variability. The authors of this review try to give a panoramic and comparative view of the key recommendations proposed by the main guidelines for the hospital care of hip fracture patients. Recommendations on the care in the acute phase are reviewed, particularly the initial hospital management, use of tools, preventive measures to avoid medical complications, surgery related aspects, treatment of usual clinical problems, and shared orthopaedic and geriatric care. Circulating and putting into practice the main recommendations will help to improve the health care provided to these patients and obtain better outcomes.     

Structural and functional roles of the N1- and N3-protons of psi at tRNA's position 39.

Pseudouridine at position 39 (Psi(39)) of tRNA's anticodon stem and loop domain (ASL) is highly conserved. To determine the physicochemical contributions of Psi(39)to the ASL and to relate these properties to tRNA function in translation, we synthesized the unmodified yeast tRNA(Phe)ASL and ASLs with various derivatives of U(39)and Psi(39). Psi(39)increased the thermal stability of the ASL (Delta T (m)= 1.3 +/- 0.5 degrees C), but did not significantly affect ribosomal binding ( K (d)= 229 +/- 29 nM) compared to that of the unmodified ASL (K (d)= 197 +/- 58 nM). The ASL-Psi(39)P-site fingerprint on the 30S ribosomal subunit was similar to that of the unmodified ASL. The stability, ribosome binding and fingerprint of the ASL with m(1)Psi(39)were comparable to that of the ASL with Psi(39). Thus, the contribution of Psi(39)to ASL stability is not related to N1-H hydrogen bonding, but probably is due to the nucleoside's ability to improve base stacking compared to U. In contrast, substitutions of m(3)Psi(39), the isosteric m(3)U(39)and m(1)m(3)Psi(39)destabilized the ASL by disrupting the A(31)-U(39)base pair in the stem, as confirmed by NMR. N3-methylations of both U and Psi dramatically decreased ribosomal binding ( K (d)= 1060 +/- 189 to 1283 +/- 258 nM). Thus, canonical base pairing of Psi(39)to A(31)through N3-H is important to structure, stability and ribosome binding, whereas the increased stability and the N1-proton afforded by modification of U(39)to Psi(39)may have biological roles other than tRNA's binding to the ribosomal P-site.     

1H-, 13C- and 31P-NMR studies of dioctanoylphosphatidylcholine and dioctanoylthiophosphatidylcholine

Coupling constants and chemical shifts were measured for dioctanoylphosphatidylcholine and its thio analogue in a CDCl3/CD3OD solvent mixture. Replacing the bridging oxygen atom of the CH-CH2-O-P portion of the phosphatidylcholine molecule with a sulfur atom affects chemical shifts and coupling constants in the glycerol backbone portion of the molecule as well as in the choline head group region. Preferred conformations about selected bonds in the phospholipids were determined from the vicinal 1H-1H, 31P-1H and 31P-13C coupling constants. A reduction of the 31P T2* (effective spin-spin relaxation time) for the thio analogue, as well as changes in the relative chemical shifts of 13C nuclei in the acyl chains, suggest a somewhat greater degree of aggregation for the thio analogue. The quadrupolar coupling constant 1J(14N-13C) for the choline methyls of either analogue, however, indicates that aggregation of these phospholipids in the CDCl3/CD3OD solvent mixture is not significant. Differences in conformation between dioctanoylphosphatidylcholine and its thio analogue may be responsible for their differences in chemical and physical properties.     

Strategies for the detection of DNA polymorphism in human populations

We develop here several models concerning strategies for detection of restriction polymorphisms in humans. These different strategies concern the numbers of individuals to test in a DNA collection, the nature of restriction enzyme to utilize, and the length of the probes. For enzyme utilization different strategies are based on (i) the nature of the restriction site; (ii) the mean length of restriction fragments obtained; (iii) the methylated cytosine characteristics in the CG doublets. Each of these approaches are tested in experimental situations.     

Zika virus infection of the placenta alters extracellular matrix proteome

Journal of Molecular Histology - Zika virus (ZIKV) infection has been associated with fetal abnormalities by compromising placental integrity, but the mechanisms by which this occurs are unknown....     

Extraintestinal Helminth Infection Reduces the Development of Colitis-Associated Tumorigenesis

Colitis-associated colorectal cancer (CAC) is one of the most common cancers and is closely related to chronic or deregulated inflammation. Helminthic infections can modulate inflammatory responses in some diseases, but their immunomodulatory role during cancer development remains completely unknown. We have analyzed the role of Taenia crassiceps-induced anti-inflammatory response in determining the outcome of CAC. We show that extraintestinal T. crassiceps infection in CAC mice inhibited colonic inflammatory responses and tumor formation and prevented goblet cell loss. There was also increased expression of IL-4 and alternatively activated macrophages markers in colonic tissue and negative immunomodulation of pro-inflammatory cytokine expression. In addition, T. crassiceps infection prevented the upregulation of β-catenin and CXCR2 expression observed in the CAC mice, which are both markers associated with CAC-tumorigenesis, and reduced the numbers of circulating and colonic CD11b⁺Ly6C^hiCCR2⁺ monocytes. Thus, immunomodulatory activities induced by helminth infections may have a role in the progression of CAC.