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Comparison of [5,5,5-2H3]leucine and [ring-2H5]phenylalanine tracers for the measurement of human apolipoprotein B100 kinetics

โœ Scribed by C. Maugeais; K. Ouguerram; P. Maugeais; C. Simoneau; J. Gardette; T. Magot; M. Krempf

Publisher
John Wiley and Sons
Year
1995
Tongue
English
Weight
380 KB
Volume
30
Category
Article
ISSN
1076-5174

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โœฆ Synopsis

Abstract

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, [5,5,5โ€^2^H~3~]leucine and [ringโ€^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 [ringโ€^2^H~5~]phenylalanine. This tracer must be used with caution in studies of specific protein synthesis.

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