Publications by authors named "Shyamala M"

Introduction: Depression is likely to be the most common psychopathology in haemodialysis patients. It might affect their adherence to treatment and is associated with increased morbidity and mortality. However, the prevalence of depression in haemodialysis patients has not been definitively determined, and it is generally underdiagnosed and undertreated.

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Health of an ecosystem is very much important as we depend on its goods and services for our existence. Because of this, we need to continuously monitor its health for human benefit and for identifying areas for improvement of our natural systems. The present study tries to assess the condition of a coastal ecosystem within the Vembanad Lake, Kerala, India, using key water quality parameters at micro-level.

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An explosion is caused by conversion of solid, liquid into gas with resultant energy release. Blast injuries of large tyres are similar to injuries resulting from landmine explosions. Most of the patients were polytraumatised, initial evaluation and management should follow ATLS.

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Objectives: To compare the effectiveness of bupivacaine with adrenaline with that of carbonated bupivacaine with adrenaline on pain, onset of anesthesia and duration of anesthesia following surgical removal of impacted mandibular third molar.

Study Design: All the patients who underwent surgical removal of impacted mandibular third molar and who fulfilled our inclusion and exclusion criteria from 1st June 2013 to 30th June 2014 were included in our study. Patients who were diagnosed as having impacted mandibular third molar were randomly allocated to two groups namely group A (bupivacaine with adrenaline), group B (carbonated bupivacaine with adrenaline).

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Background And Aim: Clitoria ternatea, a medicinal herb native to tropical equatorial Asia, is commonly used in folk medicine to treat various diseases. The aim of the present study is to evaluate the hepatoprotective and antioxidant activity of C. ternatea against experimentally induced liver injury.

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In this study, the anti-hyperlipidemic effect of aqueous extract of Pimenta officinalis (APO) was investigated in experimental rats fed with high fat diet (HFD). Hyperlipidemia in experimental rats was evidenced by a significant enhancement in the level of glycerol, triglycerides and phopholipids in serum, and also in liver and kidney tissues. HFD caused oxidative stress in these animals as shown by marked increment in the levels of thiobarbituric acid reactive substances (TBARS) and diene conjugates (CD), and a distinct diminution in reduced glutathione (GSH) content in liver and kidneys.

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A monoclonal antibody enzyme immunoinhibition assay was used to quantitate serial serum myoglobin (Mb) levels in 121 patients who had > or = 5% creatine kinase-MB (CK-MB) and suspected acute myocardial infarction (AMI). Serum Mb levels higher than 0.16 micrograms/ml were considered abnormal.

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Monoclonal antibodies (mAbs) to normal human hemoglobins (Hbs) A and F and to variant Hbs C and G-Philadelphia were conjugated to horseradish peroxidase (HRP) and used in qualitative or quantitative enzyme-linked immunosorbent assays (ELISAs). Conjugates with output molar HRP/IgG ratios close to 2.0 had higher avidity for the cognate antigens than those with ratios above or below 2.

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A murine monoclonal antibody (mAb) was generated that recognizes hemoglobin (Hb) H, the tetrameric form (beta 4) of human beta-globin chains. The antibody beta 4-1 (gamma 1, kappa) does not react with Hbs A, F, Bart's, or isolated beta chains, indicating that the antibody recognizes an epitope comprised of multiple beta chains. A simple, rapid, and sensitive enzyme immunoassay was established to detect and quantitate Hb H in hemolysates from subjects with Hb H disease.

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We have developed a murine monoclonal antibody (mAb) specific for the delta chain of hemoglobin (Hb) A2 that does not cross-react with alpha, beta, or gamma chains. The mAb reacted with Hb P-Nilotic (beta delta hybrid), but not with Hb Lepore-Boston (delta beta hybrid), indicating an epitope consisting of positions 116 (Arg) and 117 (Asn) or 125 (Gln) and 126 (Met) of the delta chain. By using this antibody, we have established a simple and rapid enzyme-linked immunosorbent assay (ELISA) for the detection and quantification of Hb A2 in adult, cord, and fetal hemolysates.

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The most common method of blood sample collection for neonatal screening programs for inherited diseases-blood spots on filter paper--is poorly suited for screening of sickle cell diseases by conventional assays because of the denaturing effects of this medium on hemoglobins that affect their electrophoretic identifications. The monoclonal antibody beta (6)-1 specifically recognizes the hemoglobin A beta-chain residue 6 (glutamic acid), that is, the normal counterpart of hemoglobins S and C, and this recognition is unaffected by changes in hemoglobins induced by filter paper storage. The beta (6)-1 immunoassay analysis of 67 prescreened samples extracted from filter paper permitted unambiguous group identification, by virtue of nonreactivity, of the pathologic sickle cell disease phenotypes SS (sickle cell anemia) and SC (sickle cell-hemoglobin C disease), along with the homozygous hemoglobin C phenotype (hemoglobin CC disease).

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To facilitate the screening of blood for the presence of hemoglobins S or C, we devised an enzyme-linked immunoassay (ELISA). The ELISA procedure incorporated a murine monoclonal antibody (mAb), beta s-1, which recognized both Hb variants but did not react with Hb A, Hb A2 or Hb F. Hemoglobins in cord or adult hemolysates were coated on the surface of wells of polystyrene microtiter plates and treated with beta s-1 mAb, followed by goat anti-mouse IgG conjugated with horseradish peroxidase.

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We have generated a murine hybridoma that secretes a monoclonal antibody (mAb) that is highly specific for hemoglobin C (HbC) [alpha 2 beta 2 6(A3)Glu----Lys] and shows no cross reactivity with HbA, HbA2, HbF, HbS, HbE, or Hb O-Arab. Using this antibody, we developed a simple and rapid enzyme linked immunosorbent assay (ELISA) technique for the detection of HbC in both adult and cord blood. The assay can be carried out using either whole blood samples or hemolysates.

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We have developed a monoclonal antibody-based enzyme immunoassay and a solid-phase radioimmunoassay for human myoglobin. Both assays are based on competition for the monoclonal antibody between the free myoglobin present in the standards or serum samples and the myoglobin coated to the wells of microtiter plates. Consequently, the absorbance at 630 nm and the radioactivity are inversely related to the concentrations of free myoglobin.

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We have prepared monospecific antibodies to Hbs D-Los Angeles, J-Baltimore, O-Arab and J-Paris-I and developed an enzyme immunoassay (ELISA) for their identification in hemolysates. Hbs in adult or cord blood hemolysates were coated to the wells of microtiter plates and reacted with the appropriate antisera followed by the detection system which contains anti-rabbit IgG/peroxidase conjugate and the substrate tetramethylbenzidine. Sixty-nine samples were tentatively considered to contain the above hemoglobin variants by isoelectrofocusing and the identity of 83% of them was confirmed by ELISA.

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We developed a monoclonal antibody against HPLC purified rat lens gamma L crystallins. This antibody was specific to both the polypeptides (19,000 and 21,000 daltons) which constituted the HPLC gamma L peak. Least reactivity was shown against gamma H (24,000 daltons).

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A monoclonal antibody (mAb) that recognizes the gamma chain of human fetal hemoglobin (Hb F) has been produced by cell hybridization techniques. The mAb reacts with Hb F (alpha 2 gamma 2), Hb Bart's (gamma 4), and Hb Kenya (gamma-beta hybrid), but does not cross-react with Hb A (alpha 2 beta 2) or Hb A2 (alpha 2 delta 2). We describe a direct enzyme-linked immunoassay (ELISA) for measurement of Hb F, in which hemoglobins from standards or from unknown hemolysates are covalently bound to the wells of microtiter plates.

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In an effort to develop a rapid screening immunoassay for the presence of hemoglobin S (Hb S) in cord blood, we have produced a hybridoma (beta s-1) secreting a monoclonal antibody (MAb) with strict specificity for Hb S over hemoglobin (Hb A). A reactivity was observed for hemoglobin C (Hb C) that was weaker than that for Hb S but still greater than 10(3) times greater than that seen for Hb A. Application of this antibody in a dot blot assay provided for a rapid (50-minute) single-step confirmatory test for Hb S, Hb C, or both in cord blood hemolysates.

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Aplysia abdominal ganglion neuron L5 is immunoreactive with an antiserum generated against the tetrapeptide Phe-Met-Arg-Phe-amide (FMRFamide); however, the specificity of this immune reagent is limited to the sequence Arg-Phe-amide. We isolated cDNA clones homologous to mRNAs specifically expressed in L5 and demonstrated that these clones do not hybridize to a previously characterized gene encoding FMRFamide. The nucleotide sequence of one of these clones, L5-67, does not encode any FMRFamide peptides but does reveal a Gly-Lys-Arg cleavage site following the amino acids Arg-Phe.

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RNA blotting and cDNA cloning techniques were used to study expression of the egg-laying hormone (ELH) gene family in the head ganglia of Aplysia californica. All head ganglia were found to express a 1800 nucleotide (nt) mRNA homologous to the ELH gene family. The nucleotide sequence of a clone isolated from a ring ganglia cDNA library demonstrates that this message encodes the ELH precursor.

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Transcription of the egg-laying hormone (ELH) gene family was examined by characterizing homologous cDNA clones from abdominal ganglion and atrial gland cDNA libraries. All cDNAs contain an exon that spans the coding region (exon III) and one or two additional exons. The tissue-specific expression of the ELH gene family was confirmed by the observation that exon III encodes the ELH precursor protein in the bag cell transcripts and either the A or B precursor proteins in the atrial gland transcripts.

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The proteins of identified cells from the Aplysia californica central nervous system were labeled with radioactive amino acids and fractionated on SDS acrylamide gels containing 6 M urea. Most of the large cells contain prominent, cell-specific protein products in the molecular weight range between 3 and 30 KD. The molecular weights of the largest specific prevalent protein products are in good agreement with the predicted molecular weights of precursors as determined from an analysis of cDNA clones homologous to mRNA's specifically expressed in several of these neurons.

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The correlation between growth conditions and centriolar antigen (Cag) expression in TC7 cells, a subline of African green monkey kidney cells, was studied. TC7 cells became quiescent when their number reached a high cell density, or when serum factors were depleted from media containing a low concentration of fetal bovine serum (FBS). There was a stoichiometric relationship between the concentration of serum present and the number of new cells produced.

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Simian virus 40 (SV 40) stimulated a host cell antigen in the centriolar region after infection of African green monkey kidney (AGMK) cells. The addition of puromycin and actinomycin D to cells infected with SV40 within 5 h after infection inhibited the stimulation of the host cell antigen, indicating that de novo protein and RNA syntheses that occurred within the first 5 h after infection were essential for the stimulation. Early viable deletion mutants of SV40 with deletions mapping between 0.

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