You limited your search to:

  Partner: UNT Libraries
 Department: Department of Biological Sciences
 Decade: 1990-1999
 Collection: UNT Theses and Dissertations
DNA Typing of HLA-B by PCR with Primer Mixes Utilizing Sequence-Specific Primers

DNA Typing of HLA-B by PCR with Primer Mixes Utilizing Sequence-Specific Primers

Date: August 1997
Creator: Chiu, Angela Chen-Yen
Description: The aim of this study was to design a resolution typing system for the HLA-B gene. This technique involves a one-step PCR reaction utilizing genomic DNA and sequence-specific primers to determine the specificity of each allele and to produce a larger primer data base ideal for serological analysis. The application of this technique to serological analysis can improve serology detection which is currently hindered by antibody cross-reactivity and the unavailability of useful typing reagents.
Contributing Partner: UNT Libraries
Nicotinic Acetylcholine Receptor α3 mRNA in Rat Visual System After Monocular Deprivation

Nicotinic Acetylcholine Receptor α3 mRNA in Rat Visual System After Monocular Deprivation

Date: August 1997
Creator: Taylor, James H. (James Harvey), 1970-
Description: In situ hybridization was used to examine effects of monocular enucleation on nicotinic acetylcholine receptor subunit cc3 mRNA in the rat dLGNand visual cortex. After 28 days postoperative, there were no significant differences in α3 mRNA density between the contralateral (deprived) and ipsilateral (non-deprived) sides. The lack of obvious effects of visual deprivation on α3 mRNA density suggests that other factors, possibly intrinsic to dLGNand visual cortex, govern the postnatal expression of α3 mRNA.
Contributing Partner: UNT Libraries
Regulation of Escherichia coli pyrBI Gene Expression in Pseudomonas fluorescens

Regulation of Escherichia coli pyrBI Gene Expression in Pseudomonas fluorescens

Date: May 1995
Creator: Shen, Weiping
Description: Pseudomonas fluorescens does not appear to regulate the enzymes of de novo pyrimidine biosynthesis at the level of gene expression. Little or no apparent repression of pyr gene expression is observed upon addition of exogenous pyrimidines to the growth medium. The Escherichia coli pyrBI genes for aspartate transcarbamoylase (ATCase) were sized down and cloned into the broad host range plasmid, pKT230. Upon introduction into a P.fluorescenspyrB mutant strain, ATCase showed repression in response to exogenously fed pyrimidine compounds. Thus, it was possible to bring about changes in pyrimidine nucleotide pool levels and in transcriptional regulation of gene expression at the same time.
Contributing Partner: UNT Libraries
Nucleotide Inhibition of Glyoxalase II

Nucleotide Inhibition of Glyoxalase II

Date: May 1999
Creator: Gillis, Glen S
Description: The glyoxalase system mediates the conversion of methylglyoxal, a toxic ketoaldehyde, to D-lactic acid. The system is composed of two enzymes, glyoxalase I (Glo-I) and glyoxalase II (Glo-II), and exhibits an absolute requirement for a catalytic quantity of glutathione (GSH). Glo-I catalyzes the isomerization of a hemithioacetal, formed non-enzymatically from methylglyoxal and GSH, to the corresponding a -D-hydroxyacid thioester, s-D-lactoylglutathione (SLG). Glo-II catalyzes the irreversible breakdown of SLG to D-lactate and GSH. We have observed that ATP or GTP significantly inhibits the Glo-II activity of tissue homogenates from various sources. We have developed a rapid, one step chromatography procedure to purify Glo-II such that the purified enzyme remains "sensitive" to inhibition by ATP or GTP (Glo-II-s). Studies indicate that inhibition of Glo-II-s by nucleotides is restricted to ATP, GTP, ADP, and GDP, with ATP appearing most effective. Kinetics studies have shown that ATP acts as a partial non-competitive inhibitor of Glo-II-s activity, and further suggest that two kinetically distinguishable forms of the enzyme exist. The sensitivity of pure Glo-II-s to nucleotide inhibition is slowly lost on storage even at -80° C. This loss is accelerated at higher temperatures or in the presence of ATP. Kinetics studies on the resultant "insensitive" ...
Contributing Partner: UNT Libraries
Nucleotide Sequence of a Bovine Arginine Transfer RNA Gene

Nucleotide Sequence of a Bovine Arginine Transfer RNA Gene

Date: May 1996
Creator: Eubanks, Aleida C. (Aleida Christine)
Description: A single plaque-pure lambda clone designated λBA84 that hybridized to a ˆ32P-labeled bovine arginine tRNA was isolated from a bovine genomic library harbored in a lambda bacteriophage vector. A 2.3-kilobase segment of this clone was found to contain an arginine transfer RNAccg gene by Southern blot hybridization analysis and dideoxyribonucleotide DNA sequencing. This gene contains the characteristic RNA polymerase III split promoter sequence found in all eukaryotic tRNAs and a potential RNA polymerase III termination site, consisting of four consecutive thymine residues, in the 3'-flanking region. Several possible cis-acting promoter elements were found within the 5'-flanking region of the sequenced gene. The function of these elements, if any, is unknown.
Contributing Partner: UNT Libraries
Subcellular Localization of N-acylphosphatidyl-ethanolamine Synthase in Cotyledons of Cotton Seedlings

Subcellular Localization of N-acylphosphatidyl-ethanolamine Synthase in Cotyledons of Cotton Seedlings

Date: December 1995
Creator: Sriparameswaran, Anuja
Description: N-acylation of phosphatidylethanolamine (PE) with free fatty acids catalyzed by N-acyl phosphatidylethanolamine (NAPE) synthase was reported in cotyledons of 24-h-old cotton seedlings. Here I report subcellular localization of this enzyme. Differential centrifugation, sucrose density gradient fractionation,aqueous two-phase partitioning and electron microscopy techniques were utilized to elucidate subcellular site(s) of NAPE synthase. Marker enzymes were used to locate organelles in subcellular fractions. Differential centrifugation indicated that NAPE synthase is present in more than one organelle and it is a membrane bound enzyme. Sucrose density gradient fractionations indicated that NAPE synthase is present in membranes derived from endoplasmic reticulum (ER),Golgi and possibly plasma membrane (PM) but not mitochondria, glyoxysomes or plastids. Aqueous two-phase partitioning experiments with cotton and spinach tissues supported these results but Goigi appeared to be the major site of NAPE synthesis. Electron microscopy of subcellular fractions was used to examine isolated fractions to provide visual confirmation of our biochemical results. Collectively, these results indicate that NAPE is synthesized in plant ER, Golgi and possibly PM.
Contributing Partner: UNT Libraries
Pyrimidine Biosynthesis in the Genus Streptomyces : Characterization of Aspartate Transcarbamoylase and Its Interaction with Other Pyrimidine Enzymes

Pyrimidine Biosynthesis in the Genus Streptomyces : Characterization of Aspartate Transcarbamoylase and Its Interaction with Other Pyrimidine Enzymes

Date: May 1998
Creator: Hughes, Lee E. (Lee Everette)
Description: Aspartate transcarbamoylase (ATCase) of Streptomyces was characterized and its interaction with other pyrimidine enzymes explored.
Contributing Partner: UNT Libraries
Assembly of Pseudomonas putida Aspartate Transcarbamoylase and Possible Roles of the PyrC' Polypeptide in the Folding of the Dodecameric Enzyme

Assembly of Pseudomonas putida Aspartate Transcarbamoylase and Possible Roles of the PyrC' Polypeptide in the Folding of the Dodecameric Enzyme

Date: May 1999
Creator: Hongsthong, Apiradee, 1970-
Description: Aspartate transcarbamoylase (ATCase) of Pseudomonas putida consists of two different polypeptides, PyrB and PyrC' (Schurr et al, 1995). The role of the PyrC' and the assembly of PyrB and PyrC' have been studied. The ATCase made in vitro of P.putida PyrB with P.putida PyrC', and of E.coli PyrB with P.putida PyrC ' were generated under two different conditions, denaturation and renaturation, and untreated. It was found that PyrC' plays a role in the enzymatic regulation by ATP, CTP and UTP. In addition to playing a role in substrate binding, the PyrB polypeptide is also involved in effector binding (Kumar et al., manuscript in preparation). The most energetically preferred form of the P.putida WT is a dodecamer with a molecular mass of 480 kDa. The ratio between the PyrB and the PyrC' is 1:1. In studies of nucleotide binding, it was discovered that the P.putida PyrB was phosphorylated by a protein kinase in the cell extract. In the presence of 20 mM EDTA, this phosphorylation was inhibited and the inhibition could be overcome by the addition of divalent cations such as Zn2+ and Mg2+. This result suggested that the phosphorylation reaction required divalent cations. In the CAD complex of eukaryotes, phosphorylations ...
Contributing Partner: UNT Libraries
Biochemical Identification of Molecular Components Required for Cyanide Assimilation in Pseudomonas fluorescens NCIMB 11764

Biochemical Identification of Molecular Components Required for Cyanide Assimilation in Pseudomonas fluorescens NCIMB 11764

Date: May 1998
Creator: Chen, Jui-Lin
Description: Utilization of cyanide as a nutritional nitrogen source in P. fluorescens NCIMB 11764 was shown to involve a novel metabolic mechanism involving nonenzymatic neutralization outside of cells prior to further enzymatic oxidation within. Several cyanide degrading enzymes were produced by NCIMB 11764 in response to growth or exposure to cyanide, but only one of these cyanide, oxygenase (CNO), was shown to be physiologically required for assimilation of cyanide as a growth substrate.
Contributing Partner: UNT Libraries
Effects of 5-hydroxytryptamine on Mouse Lumbar Motor Activity During Postnatal Development

Effects of 5-hydroxytryptamine on Mouse Lumbar Motor Activity During Postnatal Development

Date: December 1998
Creator: Lowe-Chatham, Janice E. (Janice Elaine)
Description: The lumbar motor activity in isolated spinal cords of 72 postnatal Balb/C mice aged 2, 5, 10 and 21 days (PN2-21) was electroneurographically recorded (ENG) via bilateral ventral roots following treatment with three different concentrations (25, 100 and 200 pM) of the neurotransmitter, 5-hydroxytryptamine (5-HT), i.e., serotonin, to determine its effects on spinal pattern generation.
Contributing Partner: UNT Libraries
FIRST PREV 1 2 3 4 5 NEXT LAST