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1.
Salud colect ; 10(3): 325-337, sep.-dic. 2014. tab
Article in Spanish | LILACS | ID: lil-733293

ABSTRACT

En el marco de la creciente feminización de la profesión médica en México, el artículo indaga sobre las características de este proceso para el caso de la ginecobstetricia. Considerando la feminización como un proceso de cambio, que se analiza cuantitativa y cualitativamente, el artículo se detiene en especial en las experiencias de las mujeres ginecobstetras, experiencias que se dan en el seno de una especialidad que, desde sus orígenes, funcionó como un dispositivo de control del cuerpo de las mujeres. Basado en una investigación etnográfica, el artículo combina fuentes estadísticas, de archivo y de observación de campo. El material que surge de las entrevistas muestra las experiencias y tensiones que viven las ginecobstetras en este contexto.


In the framework of an increasing feminization of the medical profession in Mexico, this article explores the characteristics of this process in the obstetrics and gynecology specialty. Understanding feminization as a process of change to be analyzed both quantitatively and qualitatively, the article focuses special attention on the experiences of female obstetrician-gynecologists within a medical specialty that has since its origins functioned as a mechanism of control over women's bodies. Based on ethnographic research, the article combines statistical and archival sources and field observation. The interviews reveal the experiences and tensions women obstetrician-gynecologists encounter in this context.


Subject(s)
Alcohol Oxidoreductases/chemistry , Alcohol Oxidoreductases/metabolism , Arginine/chemistry , Pseudomonas putida/enzymology , Alcohol Oxidoreductases/genetics , Alcohol Oxidoreductases/isolation & purification , Binding, Competitive/genetics , Catalysis , Enzyme Activation/genetics , Flavin Mononucleotide/metabolism , Kinetics , Ligands , Mandelic Acids/metabolism , Mutagenesis, Site-Directed , Phenylacetates/metabolism , Protein Binding/genetics , Pseudomonas putida/genetics , Substrate Specificity/genetics , Sulfites/metabolism
2.
Rev. colomb. biotecnol ; 12(1): 169-178, jul. 2010. tab
Article in Spanish | LILACS | ID: lil-590654

ABSTRACT

Siendo Colombia un país en el cual hay un gran desarrollo de la actividad agraria, generadora de cantidades apreciables de desechos que dan lugar a un problema ambiental, el cultivo de los hongos presenta un potencial en aplicaciones biotecnológicas que derivan de la diversidad metabólica de los mismos. Dicho potencial está tanto en la producción de los hongos como alimentos con óptimas calidades nutricionales, como en la obtención a partir de las setas de productos bioactivos que permitirían en un futuro no muy lejano contribuir a la economía del país y a la descontaminación ambiental. Dentro del reino fungi, las especies de Pleurotus pueden crecer sobre una amplia variedad de sustratos y tienen especiales propiedades para degradar los componentes lignocelulósicos presentes en mayor proporción en los residuos de la agroindustria. El objetivo del presente estudio fue el de evaluar el efecto del sustrato sobre las propiedades nutricionales o nutriceúticas de hongos del género Pleurotus. Como resultado se determinó que efectivamente la composición de los hongos en cuanto al contenido de proteínas netas, fibra, humedad, cenizas, carbohidratos y grasas totales varía con el sustrato empleado, lo que incide directamente en las propiedades antes anotadas, si se tiene en cuenta que dentro de los componentes determinados se encuentran metabolitos como polisacáridos y esteroles con bioacciones previamente reportadas. De igual manera, se encontró que estas variaciones son diferentes dependiendo de la especie.


Being Colombia a country in which there is a great development of the generating agrarian activity of appreciable quantities of waste that they give place to an environmental problem, the cultivation of the mushrooms presents a potential in biotechnical applications that derive of the metabolic diversity of the same ones. This potential is in the production of the mushrooms like in foods with good nutritional qualities. For instance in the obtaining starting from the mushrooms of bioactive products that would not allow in a very distant future to contribute to the economy of the country and the environmental decontamination. Inside the fungi Kingdom, the Pleurotus species can grow about a wide substrate variety and they have special properties to degrade the lignocelulosic component present in bigger proportions in the residuals of the agroindustry. The objective of the present study was of evaluating the substrate effect on the nutritional and/or nutriceutical quality of mushrooms of the Pleurotus gender. As a result it was determined that indeed the composition of the mushrooms as for the content of net proteins, fiber, humidity, ashes, carbohydrates and total fats, varies with the substrate used, what impacts directly in their properties, taking into account that in certain components are metabolites such as polysaccharides and sterols with bioactions previously reported. Similarly it was found that these variations are different depending on the species.


Subject(s)
Nutritive Value , Pleurotus/growth & development , Pleurotus/physiology , Pleurotus/immunology , Pleurotus/chemistry , Substrate Specificity/physiology , Substrate Specificity/genetics , Substrate Specificity/immunology
3.
Mem. Inst. Oswaldo Cruz ; 103(7): 724-730, Nov. 2008. ilus, graf, tab
Article in English | LILACS | ID: lil-498383

ABSTRACT

Protein glycosylation pathways, commonly found in fungal pathogens, offer an attractive new area of study for the discovery of antifungal targets. In particular, these post-translational modifications are required for virulence and proper cell wall assembly in Candida albicans, an opportunistic human pathogen. The C. albicans MNS1 gene is predicted to encode a member of the glycosyl hydrolase family 47, with 1,2-mannosidase activity. In order to characterise its activity, we first cloned the C. albicans MNS1 gene into Escherichia coli, then expressed and purified the enzyme. The recombinant Mns1 was capable of converting a Man9GlcNAc2 N-glycan core into Man8GlcNAc2 isomer B, but failed to process a Man5GlcNAc2-Asn N-oligosaccharide. These properties are similar to those displayed by Mns1 purified from C. albicansmembranes and strongly suggest that the enzyme is an ±1,2-mannosidase that is localised to the endoplasmic reticulum and involved in the processing of N-linked mannans. Polyclonal antibodies specifically raised against recombinant Mns1 also immunoreacted with the soluble ±1,2-mannosidases E-I and E-II, indicating that Mns1 could share structural similarities with both soluble enzymes. Due to the high degree of similarity between the members of family 47, it is conceivable that these antibodies may recognise ±1,2-mannosidases in other biological systems as well.


Subject(s)
Antibodies/immunology , Candida albicans/enzymology , Genes, Fungal , Mannosidases/genetics , Antibodies/genetics , Cloning, Molecular , Candida albicans/genetics , Candida albicans/immunology , Mannosidases/isolation & purification , Mannosidases/metabolism , Substrate Specificity/genetics
4.
Braz. j. med. biol. res ; 40(8): 1055-1064, Aug. 2007. tab, graf
Article in English | LILACS | ID: lil-456811

ABSTRACT

We recently demonstrated that the substitution of the autolysis loop (residues 143 to 154 in the chymotrypsin numbering system) of activated protein C (APC) with the corresponding loop of factor Xa (fXa) renders the APC mutant (APC/fX143-154) susceptible to inhibition by antithrombin (AT) in the presence of pentasaccharide. Our recent results further indicated, that in addition to an improvement in the reactivity of APC/fX143-154 with AT, both the amidolytic and anti-factor Va activities of the mutant APC have also been significantly increased. Since the autolysis loop of APC is five residues longer than the autolysis loop of fXa, it could not be ascertained whether this loop in the mutant APC specifically interacts with the activated conformation of AT or if a shorter autolysis loop is responsible for a global improvement in the catalytic activity of the mutant protease. To answer this question, we prepared another APC mutant in which the autolysis loop of the protease was replaced with the corresponding loop of trypsin (APC/Tryp143-154). Unlike an ~500-fold improvement in the reactivity of APC/fX143-154 with AT in the presence of pentasaccharide, the reactivity of APC/Tryp143-154 with the serpin was improved ~10-fold. These results suggest that both the length and structure of residues of the autolysis loop are critical for the specificity of the coagulation protease interaction with AT. Further factor Va inactivation studies with the APC mutants revealed a similar role for the autolysis loop of APC in the interaction with its natural substrate.


Subject(s)
Humans , Antithrombins/metabolism , Autolysis/enzymology , Blood Coagulation/genetics , Mutation/genetics , Peptide Hydrolases/genetics , Protein C/genetics , Amino Acid Sequence , Enzyme Activation , Factor Va/genetics , Factor Va/metabolism , Factor Xa/genetics , Factor Xa/metabolism , Molecular Sequence Data , Peptide Hydrolases/metabolism , Protein C/metabolism , Sequence Alignment , Substrate Specificity/genetics
5.
Experimental & Molecular Medicine ; : 145-156, 2004.
Article in English | WPRIM | ID: wpr-37854

ABSTRACT

In this study, Leishmania RNA virus 1-4 (LRV1-4) particles purified from host Leishmania guyanensis promastigotes were examined for capsid endoribonuclease. Temperature optimum for the endoribonulease activity was found to be at 37degrees C to 42degrees C and the activity was specifically inhibited by the aminoglycoside antibiotics, neomycin, kanamycin, and hygromycin and by 100 mM levels of NaCl or KCl. To determine the catalytic domain of the capsid endoribonuclease activity, three point-mutation at cysteine residues at C47S (P1), C128/ 133S (P2), and C194R (P3) were prepared and each gene was constructed into baculoviruses and expressed in Sf9 insect cells. LRV1-4 capsid N- terminus (N2 and N3) and C-terminus (C1 and C2) deletion mutants (Cadd et al., 1994) were also examined by in vitro RNA cleavage assay. The results showed that the capsid mutants; C1, C2, N3, P1, and P2 were capable of forming proper virus-like particles (VLPs) and they all possessed the specific endoribonuclease activity. However, two assembly-defective capsid mutants, N2 (N- terminus 24-amino acids deletion) and P3 mutants, did not retain the specific endoribonuclease activity. Taken together, the results suggest that at least 24 amino acids from the N-terminal region and C194 residue in LRV1-4 capsid protein are functionally important for LRV1-4 viral assembly and the capsid endoribonuclease activity may be dependent upon the properly assembled LRV1-4 virus particles.


Subject(s)
Animals , Amino Acid Substitution , Anti-Bacterial Agents/pharmacology , Baculoviridae , Capsid/enzymology , Cell Line , Cysteine/genetics , Endoribonucleases/antagonists & inhibitors , Enzyme Activation/drug effects , Hot Temperature , Insecta , Leishmania guyanensis/virology , RNA/chemistry , RNA Viruses/enzymology , Recombinant Proteins/antagonists & inhibitors , Substrate Specificity/genetics , Transduction, Genetic
6.
Braz. j. med. biol. res ; 32(7): 885-9, July 1999.
Article in English | LILACS | ID: lil-234895

ABSTRACT

The treatment of some mesenchymal malignancies has made significant gains over the past few decades with the development of effective systemic therapies. In contrast, the treatment of chondrosarcoma has been limited to surgical resection, with the most significant prognostic indicators being surgical margins and histologic grade. We have reported that MMP-1/TIMP-1 gene expression serves to prognosticate for tumor recurrence in this group of patients. This led to the hypothesis that collagenase activity facilitates cell egression from the cartilaginous matrix. In the current study we examine the specificity of collagenase gene expression in archival human chondrosarcoma samples using semi-quantitative PCR. Messenger RNA was affinity extracted and subject to reverse transcription. The subsequent cDNA was amplified using novel primers and quantitated by densitometry. Ratios of gene expression were constructed and compared to disease-free survival. The data demonstrate that the significance of the MMP-1/TIMP-1 ratio as a predictor of recurrence is confirmed with a larger number of patients. Neutrophil collagenase or MMP-8 was observed in only 5 of 29 samples. Collagenase-3 or MMP-13 was observed in all samples but the level did not correlate with disease-free survival. Since the collagenases have similar activity for fibrillar collagens and cleave the peptide in the same location, post-transcriptional regulatory mechanisms may account for the observed specificity. The determination of the MMP-1/TIMP-1 gene expression ratio not only serves to identify those patients at risk for recurrence but may also serve as a novel therapeutic avenue as an adjunct to surgical resection


Subject(s)
Humans , Bone Neoplasms/enzymology , Chondrosarcoma/enzymology , Collagenases/metabolism , Gene Expression Regulation, Enzymologic , Collagenases/analysis , Collagenases/genetics , Disease-Free Survival , DNA, Complementary/analysis , Polymerase Chain Reaction , Prognosis , Recurrence/prevention & control , RNA, Messenger/analysis , Substrate Specificity/genetics , Tissue Inhibitor of Metalloproteinase-1/analysis
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