Covalent nucleoside adducts of benzo[a]pyrene 7,8-diol 9,10-epoxides: structural reinvestigation and characterization of a novel adenosine adduct on the ribose moiety

1991 ◽  
Vol 56 (1) ◽  
pp. 20-29 ◽  
Author(s):  
Jane M. Sayer ◽  
Anju Chadha ◽  
Shiv K. Agarwal ◽  
Herman J. C. Yeh ◽  
Haruhiko Yagi ◽  
...  
Keyword(s):  
Ribose Moiety ◽  
Nucleoside Adducts

scholarly journals Purification and characterization of an oxygen-stable form of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum

1994 ◽  
Vol 302 (3) ◽  
pp. 801-806 ◽  
Author(s):  
G M Nielsen ◽  
Y Bao ◽  
G P Roberts ◽  
P W Ludden
Keyword(s):  
Fluorescence Spectra ◽  
Rhodospirillum Rubrum ◽  
Sodium Dithionite ◽  
Stable Form ◽  
Purification And Characterization ◽  
Dinitrogenase Reductase ◽  
Bivalent Metals ◽  
Overexpressing Strain ◽  
Ribose Moiety

Dinitrogenase reductase-activating glycohydrolase (DRAG) is responsible for removing the ADP-ribose moiety from post-translationally inactivated nitrogenase of Rhodospirillum rubrum. Using DRAG purified from an overexpressing strain (UR276), further properties of this enzyme were studied, including its u.v.-visible and fluorescence spectra and its stability in air. DRAG appears to require no covalently bound inorganic cofactors for its activity or regulation. Previously, purified DRAG was found to be rapidly inactivated in air. The air-catalysed lability originated with the presence of sodium dithionite and Mn2+ throughout the purification of the enzyme. This lability can be mimicked using H2O2, which is known to oxidatively inactivate proteins containing bivalent metals. Implications for the regulation of nitrogenase are discussed with respect to the lack of sensitivity to air of the regulatory enzyme, DRAG.

Chromatography and Characterization of Phenylglycidyl Ether Nucleoside Adducts

1990 ◽  
Vol 9 (3) ◽  
pp. 463-465
Author(s):  
E. G. Van den Eeckhout ◽  
E. L. Esmans ◽  
J. Claereboudt ◽  
J. Coene ◽  
M. Claeys
Keyword(s):  
Phenylglycidyl Ether ◽  
Nucleoside Adducts

Characterization of 7,12-dimethylbenz[a]anthracene-adenine nucleoside adducts

1988 ◽  
Vol 1 (4) ◽  
pp. 216-221 ◽  
Author(s):  
S. Chau Cheng ◽  
A. S. Prakash ◽  
Margaret A. Pigott ◽  
Bruce D. Hilton ◽  
John M. Roman ◽  
...  
Keyword(s):  
Nucleoside Adducts

Characterization of Nucleoside Adducts ofcis-2-Butene-1,4-dial, a Reactive Metabolite of Furan

2002 ◽  
Vol 15 (3) ◽  
pp. 373-379 ◽  
Author(s):  
Michael C. Byrns ◽  
Daniel P. Predecki ◽  
Lisa A. Peterson
Keyword(s):  
Reactive Metabolite ◽  
Nucleoside Adducts

The synthesis and characterization of α- and (β-L-fucopyranosyl phosphates and GDP fucose

1981 ◽  
Vol 59 (14) ◽  
pp. 2086-2095 ◽  
Author(s):  
Hernan A. Nunez ◽  
John V. O'Connor ◽  
Paul R. Rosevear ◽  
Robert Barker
Keyword(s):  
Coupling Constants ◽  
Synthesis And Characterization ◽  
Guanosine Diphosphate ◽  
Nmr Parameters ◽  
Ph Values ◽  
Preferential Position ◽  
Hydrolysis Of ◽  
Ribose Moiety ◽  
C Nmr

Guanosine diphosphate fucose (GDPFuc) has been synthesized chemically in an overall yield of 40% from fucose. This synthesis was made possible by increasing the yield of the key intermediate, β-L-fucopyranosyl phosphate, five-fold over that previously reported (Prihar and Behrman. Biochemistry, 12, 997 (1973)), by utilizing guanosine 5′-phosphoric di-n-butylphosphinothioic anhydride (Furusawa et al. J. Chem. Soc. Perkin Trans I, 171 (1976)) or GMP morpholdate for the synthesis of GDPFuc, and by improving the method of isolating intermediates and the final product. At pH 3, GDPFuc is degraded to GDP with a half-life of 7 h at 37 °C and 52 h at 4 °C. At pH values between 5 and 8, less than 10% is degraded after 7 days. Neither 20 mM Mn2+ nor Mg2+ in 0.2 M PIPES buffer at pH 7.5 stimulate the hydrolysis of GDPFuc. Heteronuclear, C–P and H–P coupling constants indicate that the preferential position of the phosphate moiety in both β-L-fucopyranosyl phosphate and GDPFuc is trans to C-2. In the ribose moiety of GDPFuc, the 5′-phosphate is trans to C-4. The 1Hand 13C nmr parameters of intermediates and products are reported.

scholarly journals Molecular characterization of a glycosylphosphatidylinositol-linked ADP- ribosyltransferase from lymphocytes

Blood ◽  
1996 ◽  
Vol 88 (3) ◽  
pp. 915-921 ◽  
Author(s):  
IJ Okazaki ◽  
HJ Kim ◽  
NG McElvaney ◽  
E Lesma ◽  
J Moss
Keyword(s):  
Transfer Reaction ◽  
Mammary Adenocarcinoma ◽  
Bacterial Toxin ◽  
Common Mechanism ◽  
Transferase Activity ◽  
Inhibitory Effects ◽  
Regulation Of Proliferation ◽  
Adp Ribosyltransferase ◽  
Ribose Moiety

Abstract Mono ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) to proteins. It was reported by Wang et al (J Immunol 153:4048, 1994) that incubation of mouse cytotoxic T lymphocytes (CTL) with NAD resulted in the ADP- ribosylation of membrane proteins and inhibition of cell proliferation and cytotoxicity. Treatment of CTL with phosphatidylinositol-specific phospholipase C (PI-PLC) before incubation with NAD prevented the inhibitory effects of NAD on the cells, consistent with the removal of a glycosylphosphatidylinositol (GPI)-anchored ADP-ribosyltransferase on the lymphocyte surface. We have identified and cloned a GPI-linked ADP- ribosyltransferase from Yac-1 mouse T-cell lymphoma cells. The deduced amino acid sequence of the Yac-1 transferase was 70% and 41% identical to those of the rabbit skeletal muscle and chicken heterophil, respectively. It contained three noncontiguous sequences similar to those found in several of the bacterial toxin and vertebrate ADP- ribosyltransferases. Based on crystallography of the bacterial toxins, these regions are believed to form, in part, the catalytic site consistent with a common mechanism for the ADP-ribose transfer reaction. In rat mammary adenocarcinoma (NMU) cells transformed with the Yac-1 transferase cDNA, transferase activity was present on the cell surface and was released into the medium by treatment of cells with PI-PLC. Thus, we have cloned a novel gene that has properties identical to the transferase detected in CTL, and may be involved in the NAD-dependent regulation of proliferation and cytotoxicity.

scholarly journals Molecular characterization of a glycosylphosphatidylinositol-linked ADP- ribosyltransferase from lymphocytes

Blood ◽  
1996 ◽  
Vol 88 (3) ◽  
pp. 915-921 ◽  
Author(s):  
IJ Okazaki ◽  
HJ Kim ◽  
NG McElvaney ◽  
E Lesma ◽  
J Moss
Keyword(s):  
Transfer Reaction ◽  
Mammary Adenocarcinoma ◽  
Bacterial Toxin ◽  
Common Mechanism ◽  
Transferase Activity ◽  
Inhibitory Effects ◽  
Regulation Of Proliferation ◽  
Adp Ribosyltransferase ◽  
Ribose Moiety

Mono ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) to proteins. It was reported by Wang et al (J Immunol 153:4048, 1994) that incubation of mouse cytotoxic T lymphocytes (CTL) with NAD resulted in the ADP- ribosylation of membrane proteins and inhibition of cell proliferation and cytotoxicity. Treatment of CTL with phosphatidylinositol-specific phospholipase C (PI-PLC) before incubation with NAD prevented the inhibitory effects of NAD on the cells, consistent with the removal of a glycosylphosphatidylinositol (GPI)-anchored ADP-ribosyltransferase on the lymphocyte surface. We have identified and cloned a GPI-linked ADP- ribosyltransferase from Yac-1 mouse T-cell lymphoma cells. The deduced amino acid sequence of the Yac-1 transferase was 70% and 41% identical to those of the rabbit skeletal muscle and chicken heterophil, respectively. It contained three noncontiguous sequences similar to those found in several of the bacterial toxin and vertebrate ADP- ribosyltransferases. Based on crystallography of the bacterial toxins, these regions are believed to form, in part, the catalytic site consistent with a common mechanism for the ADP-ribose transfer reaction. In rat mammary adenocarcinoma (NMU) cells transformed with the Yac-1 transferase cDNA, transferase activity was present on the cell surface and was released into the medium by treatment of cells with PI-PLC. Thus, we have cloned a novel gene that has properties identical to the transferase detected in CTL, and may be involved in the NAD-dependent regulation of proliferation and cytotoxicity.

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

AEM analysis of crystallization in Ti-based amorphous alloys

1983 ◽  
Vol 41 ◽  
pp. 270-271
Author(s):  
A.R. Pelton ◽  
A.F. Marshall ◽  
Y.S. Lee
Keyword(s):  
Magnetic Properties ◽  
Amorphous Alloys ◽  
Amorphous Materials ◽  
Isothermal Annealing ◽  
Amorphous Matrix ◽  
Nucleation And Growth ◽  
Current Interest ◽  
Amorphous Films ◽  
Electrical And Magnetic Properties

Amorphous materials are of current interest due to their desirable mechanical, electrical and magnetic properties. Furthermore, crystallizing amorphous alloys provides an avenue for discerning sequential and competitive phases thus allowing access to otherwise inaccessible crystalline structures. Previous studies have shown the benefits of using AEM to determine crystal structures and compositions of partially crystallized alloys. The present paper will discuss the AEM characterization of crystallized Cu-Ti and Ni-Ti amorphous films.Cu60Ti40: The amorphous alloy Cu60Ti40, when continuously heated, forms a simple intermediate, macrocrystalline phase which then transforms to the ordered, equilibrium Cu3Ti2 phase. However, contrary to what one would expect from kinetic considerations, isothermal annealing below the isochronal crystallization temperature results in direct nucleation and growth of Cu3Ti2 from the amorphous matrix.

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