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F Polo

Publications and source records attributed to F Polo.

At least 37 records · Page 2Linked to original sources
PubMed1998

Evaluation of the oxolinic acid--esculin--azide medium for the isolation and enumeration of faecal streptococci in a routine monitoring programme for bathing waters.

m-Enterococcus agar (m-Ent) has been generally considered the reference medium for faecal streptococci in bathing waters. However, it shows several shortcomings, and therefore it is important to test newly developed media that can guarantee more precise results. In this sense, the recently described oxolinic acid--esculin--azide agar medium (OAA) and m-enterococcus agar (m-Ent) were comparatively evaluated for the detection of faecal streptococci from seawater and fresh water. The OAA medium showed a significantly higher relative recovery percentage and specificity for both types of water than m-Ent. A similar spectrum of species was recorded from both media, Enterococcus faecium being predominant in fresh water and Enterococcus faecalis, in seawater. The superior performance of the OAA medium in both types of bathing waters, added to the fact that it does not require the use of complementary confirmative tests, makes this medium an excellent candidate to be employed for monitoring programmes.

Azides↗
PubMed1997

[Eosinophilic gastroenteritis caused by bee pollen sensitization].

A 34-year-old Spanish woman with a lifelong history of seasonal rhinoconjunctivitis and honey intolerance (pyrosis and abdominal pain) developed, 3 weeks after starting ingestion of bee pollen, astenia, anorexia, abdominal pain, diarrhoea, peripheral blood hypereosinophilia and elevated serum total IgE levels. A duodenal biopsy showed eosinophilic infiltration of the mucosal layer. Other causes of hypereosinophilia were not found. Repeated parasitological stool studies, as well as a duodenal aspirate showed negative results. Symptoms, hypereosinophilia and elevated IgE levels resolved after bee pollen ingestion was stopped. This is a typical case of eosinophilic gastroenteritis by ingestion of bee pollen in a woman with intolerance to honey bee, because the patient fulfilled the usual diagnostic criteria: gastrointestinal symptoms were present, eosinophilic infiltration of the digestive tract was demonstrated by biopsy, no eosinophilic infiltration of other organs was found and the presence of parasites was excluded. Honey intolerance and/or bee pollen administration should be considered as a cause of eosinophilic gastroenteritis.

Adult↗
PubMed1997

[A new infusion method for a prostacyclin analogue].

BACKGROUND: Iloprost, a prostaglandin I2, is chemically stable and it has been successfully used by intravenous infusion in severe limb ischemia. Usually Iloprost is diluted in 0.9% sodium chloride solution and infused intravenously for six hours each day for 28 days in hospital. METHODS: In the present study after the first three days of infusion with a traditional pump in hospital, a home pump has been utilised for the infusion of Iloprost at home. This device allows the continue infusion of Iloprost at a flow rate of 2 ml/h for six days, then the pump is filled with a new solution. The home pump consists of a protective shell in polycarbonate (10 x 12 cm), 270 ml of volume, inside there is a balloon reservoir (3 membranes) which is filled with Iloprost. The structure of Iloprost does not change into the home pump as evidenced by HPLC studies and its continue infusion allows plasmatic high levels of its active isomers during the 28 days of therapy. In 30 patients, 25 men and 5 women (mean age 61 years) with Fontaine stage IIB (6), III (5) and IV (19) POAD Iloprost has been infused with the home pump. The follow-up period was 1 to 16 months. RESULTS: The results have shown 4 major amputations and 1 death, in 9 patients complete pain relief and ulcer healing, and in 6 patients only improvement in relief of rest pain and ulcers. CONCLUSIONS: All the patients appreciated this system of infusion because they had a normal life; in addition it is less expensive because the patients stay in hospital only 3 days.

Female↗
PubMed1996

Specific depletion of the house dust mite allergen Der p 1 cereal flour prolamins.

BACKGROUND: Quantitation of Der 1 and Der 2 in dust samples by specific monoclonal antibodies is a method used increasingly to evaluate mite allergen exposure. The level of Der 1 has been proposed as a risk factor for sensitization. AIM: We report a drastic decrease in the Der 1/Der 2 ratio when dust samples are collected in bakeries. METHODS: Wheat flour and purified mites were extracted simultaneously; levels of Der p 1 and Der p 2 and cysteine protease activity were determined by ELISA and inhibition experiments. RESULTS: High titers of Der 2, but only trace amounts of Der p 1, were detected in dust collected from bakeries. Both the level and proteolytic activity of Der p 1 appeared greatly decreased when mites and wheat flour were coextracted. CONCLUSION: Group 1 protein was found to be masked by flour components, resulting in an underestimation of the mite content in bakery dust. This problem was not found for group 2 allergen.

Allergens↗
PubMed1995

Quantitation of the major allergen of several Parietaria pollens by an anti-Par 1 monoclonal antibody-based ELISA. Analysis of crossreactivity among purified Par j 1, Par o 1 and Par m 1 allergens.

BACKGROUND: Plants of the genus Parietaria, Urticaceae family, represent a major cause of pollinosis in the Mediterranean area. Different Parietaria species crossreact to a great extent, but studies on the crossreactivity among the major allergens of these pollens have not been carried out so far. OBJECTIVE: To develop an immunochemical method to quantify the major Parietaria judaica allergen, Par j 1, as well as to verify the presence of Par j 1-like proteins in different Urticaceae pollens. These proteins would be purified in order to study the cross-reactivity among them. METHODS: Immunoaffinity chromatography with a monoclonal antibody, solid-phase enzyme-linked immunoassays and SDS-PAGE. RESULTS: A monoclonal antibody-based ELISA for the quantification of Par j 1 has been developed. The assay has a sensitivity of 0.2 ng/mL and shows a high correlation with the allergenic activity of P. judaica extracts determined by radioallergosorbent assay (RAST) inhibition. By means of this assay, proteins homologous to Par j 1 were detected in P. officinalis and P. mauritanica. These proteins (Par o 1 and Par m 1, respectively) were purified by affinity chromatography using the same monoclonal antibody employed in the ELISA. Crossed-inhibition experiments demonstrated that Par j 1, Par o 1, and Par m 1, competed for the binding of specific IgE from a P. judaica-sensitive patients serum pool. CONCLUSION: The results here described suggest that shared allergenic epitopes are present in the three main allergens investigated, which may simplify the diagnosis and therapy for Parietaria allergy.

Allergens↗
PubMed1995

Quantitation of major allergens in dust samples from urban populations collected in different seasons in two climatic areas of the Basque region (Spain).

We present the results of allergen content evaluation in 80 dust samples from 31 homes of atopic patients from two climatic areas (humid and subhumid), collected in two seasons of the year (autumn and winter). Monoclonal antibody-based immunoassays were used to quantify Der p 1, Der f 1, Der 2, Lep d 1, and Fel d 1. The results were compared according to climate, season, and the type of sensitization (Pyroglyphidae mites, storage mites, or grass pollens). We underline the predominance of Dermatophagoides pteronyssinus (89% of samples) over D. farinae (16% of samples) in our environment. Der p 1 rates were higher in the humid area (Mann-Whitney P < 0.001), especially in the autumn (Wilcoxon P < 0.05). Lep d 1 was detected in 23% of samples and Lep d 1 levels were higher in the homes of patients sensitized to storage mites (Mann-Whitney P < 0.05), whereas this allergen was not detected in the homes of pollen-allergic patients. Fel d 1 was detected in nine of the 31 homes (16% of samples) although there was a cat in only one home.

Allergens↗
PubMed1994

Primary structure of Lep d I, the main Lepidoglyphus destructor allergen.

The most relevant allergen of the storage mite Lepidoglyphus destructor (Lep d I) has been characterized. Lep d I is a monomer protein of 13273 Da. The primary structure of Lep d I was determined by N-terminal Edman degradation and partially confirmed by cDNA sequencing. Sequence polymorphism was observed at six positions, with non-conservative substitutions in three of them. No potential N-glycosylation site was revealed by peptide sequencing. The 125-residue sequence of Lep d I shows approximately 40% identity (including the six cysteines) with the overlapping regions of group II allergens from the genus Dermatophagoides, which, however, do not share common allergenic epitopes with Lep d I.

Allergens↗
PubMed1993

Isolation by mAb based affinity chromatography of two Par j I isoallergens. Comparison of their physicochemical, immunochemical and allergenic properties.

We report the identification and separation of two isoallergen components of Par j I, the major allergen from Parietaria judaica pollen. First, electrophoretic conditions for consistently separating both isoforms in an SDS-PAGE system were established, and mol. wt values of 13,000 (isoallergen IA) and 10,500 (isoallergen IB) were estimated. Immunoblot, after SDS-PAGE experiments, with individual P. judaica-sensitive human sera revealed a slightly different IgE-binding pattern for each isoallergen. Four anti-Par j I mAbs were obtained from BALB/c mice immunized with a purified Par j I preparation comprising IA and IB isoallergens. Three mAbs were directed to an epitope shared by both isoallergens, and the fourth one recognized specifically one epitope on Par j IB. Dot-blot experiments with the deglycosylated allergen showed that the mAbs did not recognize the carbohydrate prosthetic group of the molecules. Affinity chromatography using the mAbs allowed the separation of the isoallergens that retained their IgE-binding ability after the purification process. Amino acid composition analyses and partial N-terminal sequencing demonstrated an extensive homology and also the existence of some structural differences between Par j I isoallergens, which is in agreement with the high, but not complete, cross-reactivity observed in competition ELISA experiments. Finally, skin prick tests performed on 28 P. judaica-sensitive patients showed that all of them recognized both isoforms and that allergenic epitopes present in Par j IA and IB are responsible for most of the allergenic activity of the whole extract.

Allergens↗
PubMed1992

Purification and characterization of Lep d I, a major allergen from the mite Lepidoglyphus destructor.

A major allergen of the storage mite Lepidoglyphus destructor (Lep d I) has been purified by affinity chromatography using an anti-Lep d I monoclonal antibody. The purity of the protein obtained by this procedure was assessed by reverse-phase HPLC. Lep d I displayed a molecular weight of 14 kD on SDS-PAGE under non-reducing conditions, and 16 kD in the presence of a reducing agent. Analytical IEF revealed a little charge microheterogeneity, showing three bands with pIs 7.6-7.8. Purified Lep d I retained IgE-binding ability, as proved by immunoblotting experiments after SDS-PAGE and RAST with individual sera from L. destructor-sensitive patients. Results from the latter technique demonstrated that 87% of L. destructor-allergic patients had specific IgE to Lep d I, and a good correlation between IgE reactivity with L. destructor extract and Lep d I was found. In addition, RAST inhibition experiments showed that IgE-binding sites on Lep d I are major L. destructor-allergenic determinants, since Lep d I could inhibit up to 75% the binding of specific IgE to L. destructor extract; on the other hand, Lep d I did not cross-react with D. pteronyssinus allergens.

Allergens↗
PubMed1992

Purification and characterization of major inhalant allergens from soybean hulls.

Proteins responsible for respiratory allergy to soybean have been purified from an extract of soybean hulls. The purification procedure combined size exclusion and reverse-phase HPLC. Two pure glycoproteins (S1 and S2) exhibiting IgE-binding ability, as demonstrated by immunoblotting and ELISA techniques, were obtained. Both proteins displayed low molecular weight values on SDS-PAGE (S1, 7.0 kD; S2 7.5 kD). Protein S1 showed charge microheterogeneity, rendering two bands at pH 6.1-6.2 on IEF, whereas S2 showed a single band at pH 6.8. Amino acid composition analyses revealed a strong homology between S1 and S2 and, as a characteristic feature, a high percentage of hydrophobic residues, mainly leucine and isoleucine. Concerning the allergenic activity, both proteins were recognized by the specific IgE from 95% of patients who suffered asthma attacks during the asthma outbreaks of 1987 and 1988 in Cartagena (Spain), caused by soybean dust. Besides, proteins S1 and S2 were able to, separately, inhibit up to 75% the binding of specific IgE to the whole extract. Moreover, purified proteins totally crossreacted, even though protein S2 seemed to be slightly more active in all the immunochemical techniques employed. Results presented allow us to conclude that both proteins are isoallergens and to name them as Gly m IA (protein S2) and Gly m IB (protein S1), according to the IUIS-allergen nomenclature system.

Allergens↗
PubMed1991

Identification of IgE-binding proteins from Lepidoglyphus destructor and production of monoclonal antibodies to a major allergen.

The allergen composition of one of the most important storage mites, Lepidoglyphus destructor, has been studied by immunodetection after SDS-PAGE with individual patient sera. An allergenic polypeptide of 14 kDa was identified with 95% of the sera. This major allergen was isolated in the supernatant of 60% ammonium sulfate salt precipitation of the whole extract, which was subsequently used to immunize BALB/c mice so as to produce monoclonal antibodies. Four mAbs recognizing molecules with IgE-binding ability were obtained. The specificity of the mAbs was assayed against different allergenic extracts, and the molecules recognized by them were characterized by immunoblotting. Two mAbs (Le5B5 and Le9E4) were directed to the 14-kDa allergen; the other two to several proteins of lesser allergenic significance.

Allergens↗
PubMed1990

Purification of Art v I, a relevant allergen of Artemisia vulgaris pollen.

An allergenic protein from Artemisia vulgaris pollen has been purified to homogeneity. Its molecular weight in native conditions is 47,000. The purified allergen, hereafter denominated Art v I, is a monomeric protein. It is a clinically relevant allergen since, at least, 70% of the individuals allergic to Artemisia vulgaris pollen have specific IgE in serum and in mast cells, demonstrated by ELISA and skin prick tests, respectively.

Allergens↗
PubMed1990

HPLC purification of the main allergen of Parietaria judaica pollen.

A two-step purification procedure of Par j I from the whole Parietaria judaica pollen extract is described. The first step consisted of gel filtration HPLC using a TSKG 3000 SW column, and 0.1% trifluoroacetic acid as the eluant. By this method, proteins were separated from the highly colored material present in the extract. Then, Par j I-containing fractions were chromatographed on a reversed-phase HPLC column (Vydac C4) using an acetonitrile gradient. This second step yielded pure Par j I as assessed by SDS-PAGE and CIE. Previously reported microheterogeneity was still observed, but amino acid analysis of various RP-HPLC fractions suggested that the heterogeneity of Par j I might not be due to changes in its primary structure. Allergenic activity of Par j I was shown to be retained after the purification procedure by several immunochemical techniques.

Allergens↗
PubMed1990

Allergenic variability in olea pollen.

Marked in vitro allergenic potency variations were observed among six different olive pollen batches as determined by RAST inhibition, in direct correlation with the content of a multimeric component of 55,000 D as analyzed by size-exclusion high performance liquid chromotography. Electrophoretical patterns displayed differences in a heterogeneous band of 20,000 D and isoelectric point around 5, which probably represents the monomeric form of the major allergen.

Allergens↗
PubMed1989

Synthesis and biological activity of photoactive derivatives of erythromycin.

Five photoactive derivatives of erythromycin have been synthesized by linking to 9(S)-aminoerythromycin either an aryl azide or a p-nitrophenyl ether. One derivative is an amide formed by reaction with (5-azido-2-formyl-phenoxy)acetic acid. Three derivatives are also amides, synthesized with 4-(p-nitroguaiacoxy)butanoic acid as a photoreactive group either directly or by interposing an amino acid (glycine or tyrosine). The last derivative is the product of the aldehyde condensation of aminoerythromycin with 10-(p-nitroguaiacoxy)decanal. Two of these derivatives can easily be made radioactive for affinity labeling studies either by reduction with [3H]borohydride (aryl azide derivative) or by 125I iodination (4-(p-nitroguaiacoxy)tyrosyl derivative). Although affected to different extents, the five erythromycin derivatives are biologically active and bind to the erythromycin-specific site on the bacterial ribosomes. In addition, the introduction of these groups changes the erythromycin inhibition pattern of peptide bond model reactions.

Aminoglycosides↗