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1.
Gynecol Obstet Fertil Senol ; 48(12): 873-882, 2020 Dec.
Artículo en Francés | MEDLINE | ID: mdl-33011381

RESUMEN

OBJECTIVE: The objective of these guidelines is to define for women at low obstetric risk modalities that respect the physiology of delivery and guarantee the quality and safety of maternal and newborn care. METHODS: These guidelines were made by a consensus of experts based on an analysis of the scientific literature and the French and international recommendations available on the subject. RESULTS: It is recommended to conduct a complete initial examination of the woman in labor at admission (consensus agreement). The labor will be monitored using a partogram that is a useful traceability tool (consensus agreement). A transvaginal examination may be offered every two to four hours during the first stage of labor and every hour during the second stage of labor or before if the patient requests it, or in case of a warning sign. It is recommended that if anesthesia is required, epidural or spinal anesthesia should be used to prevent bronchial inhalation (grade A). The consumption of clear fluids is permitted throughout labor in patients with a low risk of general anesthesia (grade B). It is recommended to carry out a "low dose" epidural analgesia that respects the experience of delivery (grade A). It is recommended to maintain the epidural analgesia through a woman's self-administration pump (grade A). It is recommended to give the woman the choice of continuous (by cardiotocography) or discontinuous (by cardiotocography or intermittent auscultation) monitoring if the conditions of maternity organization and the permanent availability of staff allow it and, after having informed the woman of the benefits and risks of each technique (consensus agreement). In the active phase of the first stage of labor, the dilation rate is considered abnormal if it is less than 1cm/4h between 5 and 7cm or less than 1cm/2h above 7cm (level of Evidence 2). It is then recommended to propose an amniotomy if the membranes are intact or an oxytocin administration if the membranes are already ruptured, and the uterine contractions considered insufficient (consensus agreement). It is recommended not to start expulsive efforts as soon as complete dilation is identified, but to let the presentation of the fetus drop (grade A). It is recommended to inform the gynecologist-obstetrician in case of nonprogression of the fetus after two hours of complete dilation with sufficient uterine dynamics (consensus agreement). It is recommended not to use abdominal expression (grade B). It is recommended to carry out preventive administration of oxytocin at 5 or 10 IU to prevent PPH after vaginal delivery (grade A). In the case of placental retention, it is recommended to perform a manual removal of the placenta (grade A). In the absence of bleeding, it should be performed 30minutes but not more than 60minutes after delivery (consensus agreement). It is recommended to assess at birth the breathing or screaming, and tone of the newborn to quickly determine if resuscitation is required (consensus agreement). If the parameters are satisfactory (breathing present, screaming frankly, and normal tonicity), it is recommended to propose to the mother that she immediately place the newborn skin-to-skin with her mother if she wishes, with a monitoring protocol (grade B). Delayed cord clamping is recommended beyond the first 30seconds in neonates, not requiring resuscitation (grade C). It is recommended that the first oral dose (2mg) of vitamin K (consensus agreement) be given systematically within two hours of birth. CONCLUSION: These guidelines allow women at low obstetric risk to benefit from a better quality of care and optimal safety conditions while respecting the physiology of delivery.


Asunto(s)
Ginecología , Partería , Parto Obstétrico , Femenino , Humanos , Oxitocina , Placenta , Embarazo
2.
Anal Bioanal Chem ; 375(6): 820-5, 2003 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-12664184

RESUMEN

The removal of heavy metals from wastewater by using activated alumina or chitosan as adsorbers was evaluated. Cd(II) and Cr(III) were employed as models of the behaviour of divalent and trivalent metal ions. The adsorption of Cd(II) and Cr(III) onto the adsorbers evaluated was studied as a function of pH, time, amount of adsorber, concentration of metal ions and sample volume. A 0.4-g portion of activated alumina can retain 0.6 mg Cr(III) and 0.2 mg Cd(II) from 20 mL sample adjusted at pH 4 and stirred for 30 min. It is therefore possible to totally decontaminate 500 mL of a waste containing 5 mg L(-1) Cd(II) and Cr(III) with 10 g alumina. On the other hand, 0.4 g chitosan can totally decontaminate 20 mL of a pH 5 solution containing up to 50 mg L(-1) Cd(II) and Cr(III). A 99.2+/-0.1% retention of Cd(II) and 83+/-1% retention of Cr(III) was obtained from 500 mL of a laboratory waste. The aforementioned strategies were applied for the minimization of analytical chemistry teaching laboratories and atomic spectrometry laboratory wastes. On comparing both adsorbers it can be concluded that chitosan is more preferable than alumina due to the reduced price of chitosan and the absence of side-pollution effects.


Asunto(s)
Óxido de Aluminio/química , Quitina/análogos & derivados , Quitina/química , Metales Pesados/química , Metales Pesados/aislamiento & purificación , Adsorción , Cadmio/análisis , Cadmio/química , Quitosano , Cromo/análisis , Cromo/química , Concentración de Iones de Hidrógeno , Eliminación de Residuos/métodos
3.
Br J Nutr ; 77(6): 885-96, 1997 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-9227186

RESUMEN

The effect of a high dose of 3-hydroxy-3-methylbutyrate (HMB, a leucine catabolite) on protein metabolism was investigated in growing male lambs fed on hay and concentrate. Concentrate was supplemented with either Ca(HMB)2 (4 g/kg) or Ca(CO3)2 in experimental (HMB) and control groups respectively. Both groups consisted of six 2-month old lambs. Three complementary methods to study protein metabolism were carried out consecutively 2.5 months after beginning the dietary treatment: whole body phenylalanine fluxes, postprandial plasma free amino acid time course and fractional rates of protein synthesis in skeletal muscles. Feeding a high dose of HMB led to a significant increase in some plasma free amino acids compared with controls. Total, oxidative and non-oxidative phenylalanine fluxes were not modified by dietary HMB supplementation. Similarly, an acute infusion of HMB, in the control group, did not change these fluxes. In skeletal muscles, fractional rates of protein synthesis were not affected by long-term dietary supplementation with HMB. Taken together our results showed that administration of a high dose of HMB to lambs was able to modify plasma free amino acid pattern without any effect on whole-body protein turnover and skeletal muscle protein synthesis.


Asunto(s)
Músculo Esquelético/metabolismo , Proteínas/metabolismo , Ovinos/metabolismo , Valeratos/farmacología , Aminoácidos/metabolismo , Animales , Dieta , Infusiones Intravenosas , Insulina/sangre , Factor I del Crecimiento Similar a la Insulina/análisis , Masculino , Fenilalanina/metabolismo , Fenilalanina/farmacología , Periodo Posprandial , Ovinos/crecimiento & desarrollo
4.
J Nutr ; 122(12): 2307-15, 1992 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-1280676

RESUMEN

We determined the effect of a 4-h leucine infusion, leading to 15-fold elevated plasma leucine concentrations, on skeletal muscle and whole-body protein synthesis in suckling lambs during the postprandial period. The [3H]phenylalanine large dose method was validated and used to quantify the fractional rates of protein synthesis (Ks in %/d) at the end of the leucine infusion. In the first experiment leucine infusion lowered plasma amino acid concentrations but did not change the Ks, the capacity for protein synthesis (Cs, mg RNA/g protein) or the efficiency of translation [g protein synthesized/(d-g RNA)] in any muscles studied or the whole body. In the second experiment the leucine-induced decreases in plasma amino acid concentrations were compensated by the simultaneous infusion of substantial amounts of amino acids. Again leucine excess did not significantly change Ks, Cs and efficiency of protein synthesis. These results indicated that leucine excess in suckling lambs during the postprandial period lowered aminoacidemia without any change of the protein synthesis rates in skeletal muscles or the whole body.


Asunto(s)
Aminoácidos/sangre , Animales Lactantes , Alimentos , Leucina/administración & dosificación , Músculos/metabolismo , Biosíntesis de Proteínas , Aminoácidos/administración & dosificación , Animales , Insulina/sangre , Cinética , Leucina/sangre , Fenilalanina/administración & dosificación , Fenilalanina/sangre , ARN/metabolismo , Ovinos , Tritio
5.
Amino Acids ; 1(1): 17-27, 1991 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-24194043

RESUMEN

These studies were undertaken to investigate the influence of the precursor amino acid on the measurement of whole-body protein turnover by the flooding-dose method. Whole-body protein synthesis rates were estimated in 70 g rats using an intravenous injection of L-(U(14)C) Threonine, L-(U(14)C) Lysine (200µmoles/100g; 0.15µCi/µmol or 1000µmoles/100 g; 0.15µCi/µmol), L-(U(14)C) Phenylalanine, L-(1(14)C) Leucine or L-(U(14)C) Histidine (200µmoles/100 g; 0.15µCi/µmol). Forty two rats were divided into seven groups. Each group received a large dose of one of the labelled amino acids. In each group, one animal was killed every 2 min between 5 and 15 min after the injection. Whole-body protein fractional rate was determined from the slope of the linear regression of Sb(t) (protein specific radioactivity) against Si'(t) ×t, where Si'(t) is the average specific radioactivity of free tissue amino acids between 0 andt. Whole-body protein fractional synthesis rates were 41.4, 25.6, 31.1, 31.4 and 22.8%/day with threonine, lysine, phenylalanine, leucine and histidine respectively. These data suggest that the estimation of whole-body protein synthesis rate varies according to the amino acid used because of the heterogeneity of the protein pool.

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