Premium
Comparison of [5,5,5‐ 2 H 3 ]leucine and [ring‐ 2 H 5 ]phenylalanine tracers for the measurement of human apolipoprotein B 100 kinetics
Author(s) -
Maugeais C.,
Ouguerram K.,
Maugeais P.,
Simoneau C.,
Gardette J.,
Magot T.,
Krempf M.
Publication year - 1995
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1190300313
Subject(s) - chemistry , phenylalanine , deuterium , hydrolysis , leucine , amino acid , acid hydrolysis , chromatography , stereochemistry , organic chemistry , biochemistry , physics , quantum mechanics
Incorporation of amino acids labeled with stable isotopes in apoliproproteins is used to estimate kinetic aspects of lipoprotein metabolism. In this study two deuterated tracers, [5,5,5‐ 2 H 3 ]leucine and [ring‐ 2 H 5 ]phenylalanine, were compared. Isolation and acid hydrolysis of apolipoproteins are required for mass spectrometric analysis. When apolipoprotein B 100 of very low density liproproteins was prepared with this procedure, a loss of deuterium was observed on deuterated phenylalanine with 10 and 6 M HCl hydrolysis but not with deuterated leucine or when 4 M HCl hydrolysis was used. This study stre sses the effect of acid hydrolysis on [ring‐ 2 H 5 ]phenylalanine. This tracer must be used with caution in studies of specific protein synthesis.