Imperial College London

Emeritus ProfessorJeremyNicholson

Faculty of MedicineDepartment of Metabolism, Digestion and Reproduction

Emeritus Professor of Biological Chemistry
 
 
 
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Contact

 

+44 (0)20 7594 3195j.nicholson Website

 
 
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Assistant

 

Ms Wendy Torto +44 (0)20 7594 3225

 
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Location

 

Office no. 665Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Nicholson:1989:10.1002/nbm.1940020207,
author = {Nicholson, JK and Gartland, KP},
doi = {10.1002/nbm.1940020207},
journal = {NMR Biomed},
pages = {77--82},
title = {1H NMR studies on protein binding of histidine, tyrosine and phenylalanine in blood plasma.},
url = {http://dx.doi.org/10.1002/nbm.1940020207},
volume = {2},
year = {1989}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The binding of histidine (His), phenylalanine (Phe) and tyrosine (Tyr) to macromolecules in blood plasma and serum has been investigated by high resolution 1H NMR spectroscopy. In single pulse and spin-echo spectra of quality control bovine serum and normal human plasma, there are no resonances in the chemical shift range to high frequency of delta = 5.3 ppm when measured in the pH (meter reading, uncorrected for the presence of 2H2O) range 3 to 8.5. On acidification of the plasma to pH less than 2.5, resonances from His and Phe are observable. In plasma from patients with Wilson's disease, weak signals from His and Tyr are seen in spin-echo spectra at pH 7.6, but increase in strength on acidification and signals from Phe appear at pH 1.8. Addition of standard solutions containing Tyr, His and especially Phe and Trp to plasma at neutral pH results in poor recovery of their expected signal intensity in spin-echo spectra. Addition of 2 M urea to bovine plasma at pH 4.5 results in the appearance of Phe signals. These data are consistent with Phe and Tyr (and to a lesser extent His) being bound in or to a macromolecular structure at neutral pH from which there is relatively slow exchange with the free solution environment. Experiments with model solutions suggest that serum albumin has a high capacity for binding aromatic amino acids (stabilized by hydrophobic interactions) at neutral pH and this is responsible for the NMR-invisibility of Tyr and Phe in blood plasma.
AU - Nicholson,JK
AU - Gartland,KP
DO - 10.1002/nbm.1940020207
EP - 82
PY - 1989///
SN - 0952-3480
SP - 77
TI - 1H NMR studies on protein binding of histidine, tyrosine and phenylalanine in blood plasma.
T2 - NMR Biomed
UR - http://dx.doi.org/10.1002/nbm.1940020207
UR - https://www.ncbi.nlm.nih.gov/pubmed/2641294
VL - 2
ER -