Related ArticlesThallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Biochemistry. 1994 Mar 22;33(11):3304-11
Authors: Aramini JM, Krygsman PH, Vogel HJ
We have examined the binding of Tl3+ to human serotransferrin and chicken ovotransferrin in the presence of carbonate and oxalate by 205Tl and 13C NMR spectroscopy. With carbonate as the synergistic anion, one observes two 205Tl NMR signals due to the bound metal ion in the two high-affinity iron-binding sites of each protein. When the same adducts are prepared with 13C-labeled carbonate, one finds two closely spaced doublets in the carbonyl region of the 13C NMR spectrum of serotransferrin; these correspond to the labeled anion directly bound to the metal ion in both sites of the protein. The analogous resonances in ovotransferrin are completely degenerate, and only one doublet can be detected. The magnitudes of the spin-spin coupling between the bound metal ion and carbonate range from 2J(205Tl-13C) approximately 270 to 290 Hz. We have used the proteolytic half-molecules of ovotransferrin and the recombinant N-terminal half-molecule of serotransferrin to assign the 205Tl and 13C NMR signals due to the bound metal ion and anion in both proteins. From titration studies, we found that Tl3+ is bound with a greater affinity at the C-terminal site of serotransferrin, whereas no site preference can be noted for ovotransferrin. When oxalate is used as the anion instead of carbonate, the 205Tl NMR signals arising from the bound metal ion in the sites of ovotransferrin are shifted downfield and become almost degenerate. A very complex pattern of resonances is observed for bound 13C2O4(2-) in the 13C NMR spectra of both proteins.(ABSTRACT TRUNCATED AT 250 WORDS)
Protocols and applications of cellular metabolomics in safety studies using precision-cut tissue slices and carbon 13 NMR.
Protocols and applications of cellular metabolomics in safety studies using precision-cut tissue slices and carbon 13 NMR.
Protocols and applications of cellular metabolomics in safety studies using precision-cut tissue slices and carbon 13 NMR.
Methods Mol Biol. 2011;691:205-25
Authors: Baverel G, Renault S, Faiz H, El Hage M, Gauthier C, Duplany A, Ferrier B, Martin G
Numerous xenobiotics are toxic to human and animal cells by interacting with their metabolism, but the precise metabolic step affected and the biochemical mechanism behind such a...
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Study of acute biochemical effects of thallium toxicity in mouse urine by NMR spectroscopy.
Study of acute biochemical effects of thallium toxicity in mouse urine by NMR spectroscopy.
Study of acute biochemical effects of thallium toxicity in mouse urine by NMR spectroscopy.
J Appl Toxicol. 2011 Jan 7;
Authors: Tyagi R, Rana P, Khan AR, Bhatnagar D, Devi MM, Chaturvedi S, Tripathi RP, Khushu S
Thallium (Tl) is a toxic heavy metal and its exposure to the human body causes physiological and biochemical changes due to its interference with potassium-dependent biological reactions. A high-resolution (1) H NMR spectroscopy based metabonomic...
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01-11-2011 11:27 PM
[NMR paper] Soft-pulsed aluminum-27 quadrupolar central transition NMR studies of ovotransferrin
Soft-pulsed aluminum-27 quadrupolar central transition NMR studies of ovotransferrin
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Soft-pulsed aluminum-27 quadrupolar central transition NMR studies of ovotransferrin
J Magn Reson. 1997 Dec;129(2):111-4
Authors: Aramini JM, Germann MW, Vogel HJ
We have employed soft (Gaussian) pulses to examine 27Al NMR signals arising from Al3+ bound to ovotransferrin. In addition to enhancing the general detectability of 27Al...
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08-22-2010 05:08 PM
[NMR paper] Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Related Articles Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin.
Biochemistry. 1994 Mar 22;33(11):3304-11
Authors: Aramini JM, Krygsman PH, Vogel HJ
We have examined the binding of Tl3+ to human serotransferrin and chicken ovotransferrin in the presence of carbonate and oxalate by 205Tl and 13C NMR spectroscopy. With carbonate as the synergistic anion, one observes two 205Tl NMR signals due to the bound metal ion in the two...
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08-22-2010 03:33 AM
[NMR paper] Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fra
Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fragments.
Related Articles Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fragments.
J Protein Chem. 1993 Dec;12(6):695-707
Authors: Huque ME, Vogel HJ
The pH-titration and dynamic behaviour of the seven lysine side chains in bovine calmodulin were studied by carbon-13 NMR. The amino groups of the calcium saturated protein and its proteolytic fragments TR1C (1-75) and TR2C (78-148) were dimethylated with carbon-13 labeled...
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08-22-2010 03:01 AM
[NMR paper] 13C NMR studies of protein motional dynamics in bovine, human, rat, and chicken ocula
13C NMR studies of protein motional dynamics in bovine, human, rat, and chicken ocular lenses.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 13C NMR studies of protein motional dynamics in bovine, human, rat, and chicken ocular lenses.
Exp Eye Res. 1993 Mar;56(3):305-16
Authors: Rydzewski JM, Wang SX, Stevens A, Serdahl C, Schleich T
The motional dynamics of lens proteins were studied by two 13C nuclear magnetic resonance (NMR) techniques sensitive to molecular...
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08-21-2010 11:53 PM
[NMR paper] Carbon-13 NMR studies of alpha-elastin.
Carbon-13 NMR studies of alpha-elastin.
Related Articles Carbon-13 NMR studies of alpha-elastin.
Ups J Med Sci. 1993;98(1):53-63
Authors: Tarnawski R, Kasperczyk J, Drózdz M
NMR investigations of model protein of elastic fibre is presented. Detailed conformation of alpha-elastin polypeptide chain is discussed by comparison with the conformation of synthetic repeat peptides of elastin. Amino acid composition of alpha-elastin obtained from C-13 NMR spectra correlates with the results of sequencing of tropoelastin.
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[NMR paper] NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-ma
NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.
Related Articles NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.
J Biol Chem. 1990 May 5;265(13):7268-72
Authors: Gettins P, Sottrup-Jensen L
NMR and ESR spectroscopies have been used to examine the plasma protease inhibitor pregnancy zone protein (PZP) and its complex with chymotrypsin. The 1H NMR spectrum of PZP shows relatively few sharp resonances, which, by analogy with human alpha...