Metabolism of [3-13C]alanine in liver of mice infected with cysticerci of Taenia crassiceps

1999 ◽  
Vol 77 (9) ◽  
pp. 1367-1372 ◽  
Author(s):  
I Corbin ◽  
B J Blackburn ◽  
M Novak
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Nmr Spectroscopy ◽  
Population Inversion ◽  
De Novo ◽  
Spin Echo ◽  
Proton Spin ◽  
Lower Percentage ◽  
Nmr Analysis ◽  
Taenia Crassiceps ◽  
Hepatic Glucose

Carbon-13-decoupled proton spin-echo nuclear magnetic resonance (NMR) spectroscopy, with and without 13C population inversion, was used to study carbon flow between the host and the parasite in the mouse - Taenia crassiceps system. This NMR analysis revealed that 2 h after intraduodenal injection of [3-13C]alanine, livers from both uninfected mice and those infected with cysticerci of T. crassiceps contained 13C label in glycogen, glucose, succinate, glutamate, alanine, and lactate. Livers of infected animals had a lower percentage of 13C in alanine, indicating increased utilization of the substrate. In addition, infected mice had a lower concentration of total hepatic glucose and glutamate. The data are consistent with an increased rate of gluconeogenesis in the liver of infected animals. Cysticerci possessed 13C label in glucose, acetate, alanine, and lactate. Since these metacestodes are unable to make glucose de novo from pyruvate, labelled glucose found in cysticerci had to be newly synthesized via the host gluconeogenic pathway and then siphoned off by the parasite.

Hepatic [2-13C]acetate metabolism by jirds infected with Echinococcus multilocularis

1999 ◽  
Vol 73 (3) ◽  
pp. 245-250 ◽  
Author(s):  
J. Schoen ◽  
M. Novak ◽  
B.J. Blackburn
Keyword(s):  
Echinococcus Multilocularis ◽  
Population Inversion ◽  
Spin Echo ◽  
Meriones Unguiculatus ◽  
Acetate Metabolism ◽  
Acetate Solution ◽  
Host Liver ◽  
Biochemical Pathways ◽  
Hepatic Glucose ◽  
End Products

Carbon-13 decoupled 1H spin echo NMR spectroscopy, with and without population inversion, was used to study carbon flow between the host, Meriones unguiculatus, and the parasite, Echinococcus multilocularis. This was accomplished by monitoring [2-13C]acetate metabolism in the liver of jirds infected with metacestodes of this parasite. Thirty minutes after injection of labelled acetate solution into the portal vein, 13C enrichment was observed in hepatic acetate, β–hydroxybutyrate, succinate, alanine, lactate and glucose. For E. multilocularis cysts, at this time,13C enrichment was observed in the same metabolites as in livers and, in addition, citrate. At 120 min there was a significant decrease in the amount of label present in all hepatic metabolites whereas more label was found in the majority of the parasite metabolites. The results confirm that exogenous acetate, through randomization of the 13C in biochemical pathways of host liver, ends up in hepatic glucose. As this biosynthetic route is not available to the parasite, the presence of 13C enriched glucose in the cysts clearly indicates that the parasite is siphoning off glucose that is newly synthesized by the host. At 120 min some of this labelled glucose was stored in parasite glycogen whereas some of it had been catabolized to succinate, alanine, lactate and acetate, end products which are excreted back into the host.

scholarly journals Nuclear Magnetic Resonance seq (NMRseq): A New Approach to Peptide Sequence Tags

Toxins ◽  
2018 ◽  
Vol 10 (11) ◽  
pp. 437 ◽  
Author(s):  
David Wilson ◽  
Norelle L. Daly
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Nmr Spectroscopy ◽  
Magnetic Resonance ◽  
De Novo ◽  
Three Dimensional ◽  
Peptide Sequence ◽  
Dimensional Structure ◽  
Amino Acid Type ◽  
Three Dimensional Structure ◽  
Nuclear Magnetic

Structural analysis of peptides with nuclear magnetic resonance (NMR) spectroscopy generally relies on knowledge of the primary sequence to enable assignment of the resonances prior to determination of the three-dimensional structure. Resonance assignment without knowledge of the sequence is complicated by redundancy in amino acid type, making complete de novo sequencing using NMR spectroscopy unlikely to be feasible. Despite this redundancy, we show here that NMR spectroscopy can be used to identify short sequence tags that can be used to elucidate full-length peptide sequences via database searching. In the current study, we have used this approach to identify conotoxins from the venom of the cone snail Conus geographus and determined the three-dimensional structure of a member of the I3 superfamily. This approach is most likely to be useful for the characterization of disulfide-rich peptides, such as those that were chosen for this study, as they generally have well-defined structures, which enhances the quality of the NMR spectra. In contrast to other sequencing methods, the lack of sample manipulation, such as protease digestion, allows for subsequent bioassays to be carried out using the native sample used for sequence identification.

Double Spin Echo Volume Selective NMR Spectroscopy with a 1.5 T Whole Body Imager

1989 ◽  
Vol 44 (12) ◽  
pp. 1183-1186 ◽  
Author(s):  
W.-I. Jung ◽  
O. Lutz
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Nmr Spectroscopy ◽  
High Performance ◽  
Spin Echo ◽  
Whole Body ◽  
Resonance Spectroscopy ◽  
Minimal Size ◽  
Double Spin ◽  
Localization Sequence ◽  
Leg Muscle

Abstract For volume selective nuclear magnetic resonance spectroscopy with protons a modified version of the double spin echo method has been implemented on a 1.5 T whole body imager. The high performance of the localization sequence has been verified with phantoms and tissue. A spectral resolution of about 2 · 10-8 was obtained. The volume elements are well shaped and positioned, the minimal size was 2.2 cm3. Spectra of porcine leg muscle tissue with different echo times are presented.

Introduction of LTCC Technology in Fabrication of the Planar Microcoils for NMR Spectroscopy

2013 ◽  
Vol 685 ◽  
pp. 362-366 ◽  
Author(s):  
Pero Krivic
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Nmr Spectroscopy ◽  
Magnetic Resonance ◽  
Low Temperature ◽  
High Sensitivity ◽  
The Other ◽  
Nmr Analysis ◽  
Material Technology ◽  
High Quality ◽  
Polymer Substrates

Usage of planar microcoils in nuclear magnetic resonance (NMR) analysis of volume-limited chemical and biological samples has been widespread over the decades, since these microcoils obtain high sensitivity and resolution in localized units of volume. On the other hand, low-temperature co-fired ceramic (LTCC) materials exhibit highly reliable and advantageous properties in the radio frequency (RF) working area. In this work, author tries to incorporate this prosperous material technology in to design of high quality NMR microcoils, which were so far fabricated on the glass or polymer substrates. Set of few ceramic substrate microcoils is fabricated and characterized with detailed description of fabrication process in this paper.

Conductivity Studies of Schiff Base Ligands Derived from O-Phenylenediamine and Their Co(II) and Zn(II) Complexes

2015 ◽  
Vol 12 (2) ◽  
pp. 13
Author(s):  
Muhamad Faridz Osman ◽  
Karimah Kassim
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Fourier Transform ◽  
Schiff Base ◽  
Nmr Spectroscopy ◽  
Magnetic Resonance ◽  
Impedance Spectroscopy ◽  
Ftir Spectroscopy ◽  
Coordination Complexes ◽  
Frequency Range ◽  
Schiff Base Ligands

The coordination complexes of Co(II) and Zn(II) with Schiff bases derived from o-phenylenediamine and substituted 2-hydroxybenzaldehyde were prepared All compounds were characterized by Fourier transform infrared (FTIR) spectroscopy and Nuclear magnetic resonance (NMR) spectroscopy elemental analyzers. They were analyzed using impedance spectroscopy in the frequency range of 100Hz-1 MHz. LI and L2 showed higher conductivity compared to their metal complexes, which had values of 1.3 7 x 10-7 and 6.13 x 10-8 S/cm respectively. 

Biological NMR Spectroscopy

1997 ◽  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Nmr Spectroscopy ◽  
Magnetic Resonance ◽  
Magnetic Resonance Spectroscopy ◽  
State Of The Art ◽  
Critical Assessment ◽  
Resonance Spectroscopy ◽  
History Of ◽  
Structure Of Proteins

This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.

Unravelling the dissolution mechanism of polyphosphate glasses by 31P NMR spectroscopy: ligand competition and reactivity of intermediate complexes

2021 ◽  
Author(s):  
Dahiana Andrea Avila Salazar ◽  
Peter Bellstedt ◽  
Atsuhiro Miura ◽  
Yuki Oi ◽  
Toshihiro Kasuga ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Solid State ◽  
Nmr Spectroscopy ◽  
Biomedical Applications ◽  
Structural Changes ◽  
31P Nmr ◽  
Dissolution Mechanism ◽  
31P Nmr Spectroscopy ◽  
Glass Dissolution ◽  
Polyphosphate Glasses

Phosphate glass dissolution can be tailored via compositional and subsequent structural changes, which is of interest for biomedical applications such as therapeutic ion delivery. Here, solid-state 31P nuclear magnetic resonance...

scholarly journals Exploring the Structural Chemistry of Pyrophosphoramides: N,N′,N″,N‴-Tetraisopropylpyrophosphoramide

Chemistry ◽  
2021 ◽  
Vol 3 (1) ◽  
pp. 149-163
Author(s):  
Duncan Micallef ◽  
Liana Vella-Zarb ◽  
Ulrich Baisch
Keyword(s):  
Crystal Structure ◽  
Mass Spectrometry ◽  
Nuclear Magnetic Resonance ◽  
Hydrogen Bonding ◽  
Nmr Spectroscopy ◽  
Ir Spectroscopy ◽  
Room Temperature ◽  
Intermolecular Hydrogen Bonding ◽  
X Ray Diffraction ◽  
X Ray

N,N′,N″,N‴-Tetraisopropylpyrophosphoramide 1 is a pyrophosphoramide with documented butyrylcholinesterase inhibition, a property shared with the more widely studied octamethylphosphoramide (Schradan). Unlike Schradan, 1 is a solid at room temperature making it one of a few known pyrophosphoramide solids. The crystal structure of 1 was determined by single-crystal X-ray diffraction and compared with that of other previously described solid pyrophosphoramides. The pyrophosphoramide discussed in this study was synthesised by reacting iso-propyl amine with pyrophosphoryl tetrachloride under anhydrous conditions. A unique supramolecular motif was observed when compared with previously published pyrophosphoramide structures having two different intermolecular hydrogen bonding synthons. Furthermore, the potential of a wider variety of supramolecular structures in which similar pyrophosphoramides can crystallise was recognised. Proton (1H) and Phosphorus 31 (31P) Nuclear Magnetic Resonance (NMR) spectroscopy, infrared (IR) spectroscopy, mass spectrometry (MS) were carried out to complete the analysis of the compound.

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