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Articles 1 - 4 of 4
Full-Text Articles in Amino Acids, Peptides, and Proteins
Regulation Of Queuine Insertion Into Transfer Rna: Effects Of Tumor Promoters, Bonnie Jean Brooks
Regulation Of Queuine Insertion Into Transfer Rna: Effects Of Tumor Promoters, Bonnie Jean Brooks
Chemistry & Biochemistry Theses & Dissertations
The purpose of this study was to treat normal human fibroblasts with known tumor promoters and observe queuine modification of tRNA. The queuine insertion enzyme, tRNAguanine ribosyltransferase, was studied in vivo and in vitro. Tumor promoter-treated human fibroblast cultures exhibited variable queuine-insertion rates with a transient inhibition that correlated with variable levels of queuine modified tRNA over time in culture from passages 3 — 8. In contrast the in vitro studies showed that phorbol cetera and saccharin actually increased insertion with strong evidence indicating phosphorylation as a positive modulating force of the enzyme activity. It is proposed that chronic stimulation …
Effect Of Photoperiod On Developmental Morphology And Enolase Isoenzyme Immunohistochemistry In Rat And Djungarian Hamster Superficial Pineal Glands, Chalmer D. Mcclure
Effect Of Photoperiod On Developmental Morphology And Enolase Isoenzyme Immunohistochemistry In Rat And Djungarian Hamster Superficial Pineal Glands, Chalmer D. Mcclure
Loma Linda University Electronic Theses, Dissertations & Projects
The best understood functional activity of the pineal gland is its diurnal production of melatonin in response to environmental lighting cues. Several enzymes of the melatonin pathway respond to daily photoperiod changes, for example hydroxyindole-O-methyltransferase (HIOMT) and serotonin N-acetyltransferase (SNAT). Increased levels of the glycolytic enzyme neuron-specific enolase (NSE) are thought to reflect increased physiological demands placed on neurons and neuroendocrine tissues. Homodimer non-neuronal enolase isoenzyme (NNE) is immunolocalized to cells, and the hybrid enolase (consisting of subunits from NSE and NNE) has been seen in cerebellar stellate and basket cells. Although not rate limiting, concentrations of both NSE and …
Collagen Binding Proteins Derived From The Embryonic Fibroblast Cell Surface Recognize Arginine-Glycine-Aspartic Acid, Roy C. Ogle, Charles D. Little
Collagen Binding Proteins Derived From The Embryonic Fibroblast Cell Surface Recognize Arginine-Glycine-Aspartic Acid, Roy C. Ogle, Charles D. Little
Medical Diagnostics & Translational Sciences Faculty Publications
Several cell surface proteins (Mr = 120,000, 90,000, 63,000 and 47,000) apparently integral to embryonic fibroblast plasma membranes were extracted with detergent and isolated by collagen affinity chromatography. Certain of these proteins (Mr = 120,000, 90,000, and 47,000) were specifically eluted from collagen affinity columns by synthetic peptides containing the amino acid sequence arginyl-glycyl-aspartic acid (RGD). These data show that a number of collagen binding proteins exist on the embryonic fibroblast cell surface. Some of the proteins may be collagen receptors binding to RGD sequences in the collagen molecule while at least one of the proteins (Mr = 63,000) recognizes …
The Amino Acid Sequence Of The Adult Sumatran Tiger (Panthera Tigris, Carnivora) Hemoglobins, Meeno Jahan, Aftab Ahmed, Gerhard Braunitzer, Reinhard Göltenboth
The Amino Acid Sequence Of The Adult Sumatran Tiger (Panthera Tigris, Carnivora) Hemoglobins, Meeno Jahan, Aftab Ahmed, Gerhard Braunitzer, Reinhard Göltenboth
Pharmacy Faculty Articles and Research
The complete amino-acid sequences of the hemoglobins from the adult Sumatran tiger (Panthera tigris sumatrae) have been determined on automatic liquid- and gas-phase sequenators. The globin chains were isolated by reverse phase HPLC on a column of Nucleosil-C4.7V-Acetylserine was detected by FAB-mass spectroscopy as TV-terminal amino acid residue of the βI chain. Comparing the sequences of the globin chains of the tiger with that of human Hb-A, 23 substitutions were recognized in the a, 29 in βI and 28 in the βII chain.