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Biomedical subjects

R Tyagi

Publications and source records attributed to R Tyagi.

14 recordsLinked to original sources
PubMed2006

Efficacy of three doses of tramadol with bupivacaine for caudal analgesia in paediatric inguinal herniotomy.

BACKGROUND: This study was designed to evaluate the analgesic efficacy of three doses of tramadol, administered caudally with bupivacaine, in providing postoperative pain relief in children. METHODS: Eighty children, aged between 2 and 8 yr, undergoing inguinal herniotomy were randomly allocated to receive bupivacaine 0.25% 0.75 ml kg(-1) (Group B; n=20), bupivacaine 0.25% 0.75 ml kg(-1) with tramadol 1 mg kg(-1) (Group BT1; n=20), bupivacaine 0.25% 0.75 ml kg(-1) with tramadol 1.5 mg kg(-1) (Group BT1.5; n=20), or bupivacaine 0.25% 0.75 ml kg(-1) with tramadol 2 mg kg(-1) (Group BT2; n=20) by the caudal route immediately after induction of general anaesthesia. Heart rate, arterial pressure and oxygen saturation were monitored. Postoperative pain was assessed at regular intervals for 24 h using All India Institute of Medical Sciences pain score. Analgesia was supplemented whenever pain score was >or=4. Duration of analgesia and requirement for additional analgesics was noted. RESULTS: Duration of analgesia was longer in Group BT2 [(mean (SD) 12 (0.9) h] compared with Group B [4 (1) h], Group BT1 [8 (0.9) h], or Group BT1.5 [11 (1) h]; all P<0.001. Total consumption of rescue analgesic was significantly lower in group BT2 compared with other groups (P<0.001). There were no significant changes in heart rate, arterial pressure and oxygen saturation between groups. Adverse effects were not observed. CONCLUSIONS: Caudal tramadol 2 mg kg(-1), combined with bupivacaine 0.25% 0.75 ml kg(-1), provided longer duration of postoperative analgesia and reduced requirement for rescue analgesic compared with tramadol 1 mg kg(-1) or 1.5 mg kg(-1) in children undergoing inguinal herniotomy.

Acetaminophen↗
PubMed2003

Protective role of certain chemicals against UV-B-induced damage in the nitrogen-fixing cyanobacterium, Nostoc muscorum.

The protective effects of L-cysteine, ascorbic acid, reduced glutathione, L-tryptophan, and sodium pyruvate against UV-B-induced damages were studied in the nitrogen-fixing cyanobacterium, Nostoc muscorum. When added to the culture suspension during UV-B treatment, these chemicals caused a significant protective effect on survival and growth of the organism. Sodium pyruvate conferred the strongest protection whereas the weakest effect was elicited by tryptophan. A 20 min exposure of a culture suspension to UV-B completely inactivated nitrogenase activity but the inactivation was strongly prevented by exogenous addition of ascorbic acid or reduced glutathione during UV-B exposure, and weakly prevented by pyruvate, cysteine and tryptophan. In vivo nitrate reductase activity was not completely lost even after 80 min of UV-B exposure, and addition of the test chemicals did not confer any significant protection to this enzyme. Whereas (14)CO(2) uptake was drastically inhibited (78% inhibition) by 30 min exposure to UV-B in the absence of any test chemical, about 76% activity remained when the UV-B exposure was given to cultures in the presence of ascorbic acid. These results suggest that the damaging effects of UV-B are substantially minimized by certain reducing agents, the protective effect being particularly strong on the O(2) sensitive enzyme, nitrogenase. Presence of these chemicals in their natural habitat or inside the cells of living organisms may partially protect/repair the damaging effects of UV-B radiation.

Ascorbic Acid↗
PubMed2001

The gene for the axonal cell adhesion molecule TAX-1 is amplified and aberrantly expressed in malignant gliomas.

The human TAX-1 gene encodes a Mr 135,000 glycoprotein that is transiently expressed on the surface of a subset of neurons during development and is involved in neurite outgrowth. The TAX-1 gene has been mapped to a region on chromosome 1 that has been implicated in microcephaly and the Van der Woude syndrome. Using restriction landmark genome scanning to search for amplified genes in gliomas, we found TAX-1 to be amplified in 2 high-grade gliomas among a group of 26 gliomas investigated. Real-time reverse transcription-quantitative PCR analysis detected high levels of TAX-1 mRNA in glial tumors, even in the absence of TAX-1 gene amplification. Immunohistochemical analysis revealed abundant levels of TAX-1 in neoplastic glial cells of glioblastoma multiforme tumors. Because glial tumors are highly invasive and in view of the role of TAX-1 in neurite outgrowth, we investigated the potential role of TAX-1 in glioma cell migration. Using an in vitro assay, we found that the migration of glioma tumor cells is profoundly reduced in the presence of either an anti-TAX-1 antibody or a TAX-1 antisense oligonucleotide. Our findings suggest that TAX-1 plays a role in glial tumorigenesis and may provide a potential target for therapeutic intervention.

Blotting, Northern↗
PubMed2000

Enhancement of catalytic efficiency of enzymes through exposure to anhydrous organic solvent at 70 degrees C. Three-dimensional structure of a treated serine proteinase at 2.2 A resolution.

The enzyme behavior in anhydrous media has important applications in biotechnology. So far chemical modifications and protein engineering have been used to alter the catalytic power of the enzymes. For the first time, it is demonstrated that an exposure of enzyme to anhydrous organic solvents at optimized high temperature enhances its catalytic power through local changes at the binding region. Six enzymes: proteinase K, wheat germ acid phosphatase, alpha-amylase, beta-glucosidase, chymotrypsin and trypsin have been exposed to acetonitrile at 70 degrees C for three hours. The activities of these enzymes were found to be considerably enhanced. In order to understand the basis of this change in the activity of these enzymes, the structure of one of these treated enzymes, proteinase K has been analyzed in detail using X-ray diffraction method. The overall structure of the enzyme is similar to the native structure in aqueous environment. The hydrogen bonding system of the catalytic triad is intact after the treatment. However, the water structure in the substrate binding site undergoes some rearrangement as some of the water molecules are either displaced or completely absent. The most striking observation concerning the water structure pertains to the complete deletion of the water molecule which occupied the position at the so-called oxyanion hole in the active site of the native enzyme. Three acetonitrile molecules were found in the present structure. All the acetonitrile molecules are located in the recognition site. The sites occupied by acetonitrile molecules are independent of water molecules. The acetonitrile molecules are involved in extensive interactions with the protein atoms. All of them are interlinked through water molecules. The methyl group of one of the acetonitrile molecules (CCN1) interacts simultaneously with the hydrophobic side chains of Leu-96, Ile-107, and Leu-133. The development of such a hydrophobic environment at the recognition site introduces a striking conformation change in Ile-107 by rotating its side chain about C(alpha)--C(beta) bond by 180 degrees to bring about the delta-methyl group within the range of attractive van der Waals interactions with the methyl group of CCN1. A similar change has earlier been observed in proteinase K when it is complexed to a substrate analog lactoferrin fragment.

Acetonitriles↗
PubMed1998

GAC1, a new member of the leucine-rich repeat superfamily on chromosome band 1q32.1, is amplified and overexpressed in malignant gliomas.

We have used two-dimensional electrophoresis of enzyme-digested genomic DNA to identify a novel gene GAC1, which maps at 1q32.1 and which is overexpressed in malignant gliomas in which it is amplified. GAC1 encodes a protein which belongs to the leucine-rich repeat superfamily. Amplification and overexpression of GAC1 was demonstrated in two of eight tumors where amplifications were previously evidenced by comparative genomic hybridization (one glioblastoma multiforme and one anaplastic astrocytoma), and in one of eight unselected glioblastomas multiforme. GAC1 exhibits sequence homology with other proteins which function as cell-adhesion molecules or as signal transduction receptor and is a likely candidate for the target gene in the 1q32.1 amplicon in malignant gliomas.

Amino Acid Sequence↗
PubMed1998

Chemical modification and chemical cross-linking for protein/enzyme stabilization.

The protein function as well as its stability is governed by the amino acid sequence which in turn defines the collective noncovalent interactions leading to its specific conformation. Hence, it is not surprising that chemical modification with monofunctional and bifunctional reagents (the latter is called chemical cross-linking) causes structural changes (sometimes even subtle) which can result in significant changes in the stability. This review, while recapitulating the early lessons, analyses recent work (including work from authors' laboratory) involving these twin approaches for protein stabilization. In the case of chemical modification, both surface hydrophilization and enhancing surface hydrophobicity are reported to have enhanced protein stability in different cases. For cross-linking, the nature, span, and position of the cross-link are important factors in the stabilization achieved. It is also pointed out that in the case of aqueous-organic cosolvent mixtures, protein stability may depend upon the nature of the organic solvents. In the case of polyphenol oxidase and trypsin (at least), it is possible to choose "good" solvents on the basis of the Polarity index of the solvent.

Cross-Linking Reagents↗
PubMed1998

Synthesis and anti-inflammatory activity of some potential cyclic phenothiazines.

Some new schiff's bases (IVa-IVe), thiazolidinones (Va-Ve), delta 2-triazolines (VIa-VIe) and formazans (VIIa-VIIe) of 2-chlorophenothiazine have been synthesized and screened against Carrageenin induced oedema in albino rats. Some compounds of the series have shown promising activity. The most active compound is 2-chloro-10[5-(2-fluorophenyl-2-oxo-4 thiazolidin-1-yl)-amino acetyl] phenothiazine was found to be most potent. This compound (Vb) was further evaluated in detail and compared with phenylbutazone for its relative anti inflammatory potency (ED50), ulcerogenic liabilities (UD50) and acute toxicity (ALD50). It was found to be almost comparable to phenylbutazone as regards anti-inflammatory activity was concerned but and minimum ulcerogenic liability and cardiovascular effects. Hence, it seems promising as an anti-inflammatory agent in our preliminary studies.

Administration, Oral↗
PubMed1998

Carbodi-imide coupling of enzymes to the reversibly soluble insoluble polymer Eudragit S-100.

The coupling of proteins and enzymes to soluble-insoluble polymers by carbodi-imide can be performed by using numerous variations of the protocol. This protocol has been investigated for the coupling of five different enzymes, namely wheatgerm acid phosphatase, beta-glucosidase, beta-galactosidase, trypsin and xylanase, to an enteric methacrylate polymer Eudragit S-100. The following results were found. (1) The activity of the bioconjugate was critically dependent on the physical state of the polymer and the pH of the coupling reaction. For example, in the case of wheatgerm acid phosphatase, the activity of the bioconjugate was 49% when coupling was performed at pH 7.2 and 67% when coupling was performed at pH 4. 5. With beta-galactosidase the corresponding values were 57% and 23% and with beta-glucosidase they were 57% and 52% respectively. (2) In some cases, such as beta-glucosidase and beta-galactosidase, it might be necessary to remove excess carbodi-imide before the addition of the enzyme to the activated matrix. (3) In most of the cases investigated, a sig-nificant amount of the enzyme (more than 90%) could be bound to the matrix merely by adsorption. (4) More importantly, after the carbodi-imide coupling procedure, a sufficient fraction of the bound enzyme could be eluted off the matrix, indicating that this was merely adsorbed and not covalently coupled.

Acid Phosphatase↗
PubMed1995

Immobilization of Aspergillus niger xylanase on magnetic latex beads.

Xylanase from Pectinex 3XL was purified 70-fold by precipitation with an enteric polymer, Eudragit S-100. The purified xylanase was immobilized on magnetic latex beads via carbodi-imide coupling. The immobilized preparation showed 80% of the total activity bound to the beads. The pH optimum remained unchanged at 6.0 and the Km increased from 0.25 g/100 ml (free enzyme) to 0.39 g/100 ml on immobilization. Immobilization resulted in significant thermal stability at 60 degrees C. The time course of hydrolysis of xylan at 60 degrees C by free enzyme as well as immobilized enzyme was also studied.

Aspergillus niger↗
PubMed1995

Purification and characterization of an acid phosphatase from Arachis hypogaea.

An acid phosphatase from Arachis hypogaea (peanuts) has been purified. The electrophoretically homogeneous enzyme preparation is free of any phophodiesterase activity. The enzyme has a molecular weight of 120,000. Among the various phosphomonoesters tested, p-nitrophenylphosphate was found to be its most effective substrate. The Km for p-nitrophenylphosphate was 1.21 mM at pH 5.0 and 25 degrees C. The enzyme was thermostable and did not loose activity after 1 hr at 50 degrees C.

Acid Phosphatase↗
PubMed1994

An insoluble aggregate of commercially available bovine serum albumin shows antiproteolytic activity.

Chemical aggregation of bovine serum albumin by extensive chemical crosslinking with glutaraldehyde yielded an insoluble protein preparation with significant antiproteolytic activity. This was presumably due to the presence of alpha 2-macroglobulin in bovine serum albumin preparations. Chemical crosslinking of bovine serum albumin under optimum conditions was found to increase its antitryptic activity by about four times. The results indicate that enhanced rigidity of alpha 2-macroglobulin structure increases its antitryptic activity.

Animals↗
PubMed1992

Differential effect of ultraviolet-B radiation on certain metabolic processes in a chromatically adapting Nostoc.

The impact of UV-B radiation on growth, pigmentation and certain physiological processes has been studied in a N2-fixing chromatically adapting cyanobacterium, Nostoc spongiaeforme. A brownish form (phycoerythrin rich) was found to be more tolerant to UV-B than the blue-green (phycocyanin rich) form of N. spongiaeforme. Continuous exposure to UV-B (5.5 W m-2) for 90 min caused complete killing of the blue-green strain whereas the brown strain showed complete loss of survival after 180 min. Pigment content was more strongly inhibited in the blue-green strain than in the brown. Nitrogenase activity was completely abolished in both strains within 35 min of UV-B treatment. Restoration of nitrogenase occurred upon transfer to fluorescent or incandescent light after a lag of 5-6 h, suggesting fresh synthesis of nitrogenase. Unlike the above processes, in vivo nitrate reductase activity was stimulated by UV-B treatment, the degree of enhancement being significantly higher in the blue-green strain. Like the effect of UV-B on nitrogenase, 14CO2 uptake was also completely abolished by UV-B treatment in both strains. Our findings suggest that UV-B may produce a deleterious effect on several metabolic activities of cyanobacteria, especially in cells lacking phycoerythrin. Strains containing phycoerythrin appear to be more tolerant to UV-B, probably because of their inherent property of adapting to a variety of light qualities.

Adaptation, Physiological↗
PubMedDate not supplied

Enhancement of catalytic activity of enzymes by heating in anhydrous organic solvents: 3D structure of a modified serine proteinase at high resolution.

For the first time, it is demonstrated that exposure of an enzyme to anhydrous organic solvents at optimized high temperature enhances its catalytic power through local changes at the binding region. Six enzymes, namely, proteinase K, wheat germ acid phosphatase, alpha-amylase, beta-glucosidase, chymotrypsin and trypsin were exposed to acetonitrile at 70 degrees C for three hr. The activities of these enzymes were found to be considerably enhanced. In order to understand the basis of this change in the activity of these enzymes, proteinase K was analyzed in detail using X-ray diffraction method. The overall structure of the enzyme was found to be similar to the native structure in aqueous environment. The hydrogen bonding system of the catalytic triad remained intact after the treatment. However, the water structure in the substrate binding site underwent some rearrangement as some of the water molecules were either displaced or completely absent. The most striking observation concerning the water structure was the complete deletion of the water molecule which occupied the position at the so-called oxyanion hole in the active site of the native enzyme. Three acetonitrile molecules were found in the present structure. All the acetonitrile molecules were located in the recognition site. Interlinked through water molecules, the sites occupied by acetonitrile molecules were independent of water molecules. The acetonitrile molecules are involved in extensive interactions with the protein atoms. The methyl group of one of the acetonitrile molecules (CCN1) interacts simultaneously with the hydrophobic side chains of Leu 96, Ile 107 and Leu 133. The development of such a hydrophobic environment at the recognition site introduced a striking conformation change in Ile 107 by rotating its side chain about C alpha-C beta bond by 180 degrees to bring about the delta-methyl group within the range of attractive van der Waals interactions with the methyl group of CCN1. A similar change had earlier been observed in proteinase K when it was complexed to a substrate analogue, lactoferrin fragment.

Acetonitriles↗