TY - JOUR
T1 - Phenylalanine conversion to tyrosine
T2 - Comparative determination with l-[ring-2H5]phenylalanine and l-[1-13C]phenylalanine as tracers in man
AU - Marchini, J. S.
AU - Castillo, L.
AU - Chapman, T. E.
AU - Vogt, J. A.
AU - Ajami, A.
AU - Young, V. R.
N1 - Funding Information:
From the Laboratory of Human Nutrition, Clinical Research Center and School of Science, Massachusetts Institute of Technology. Cambridge; the Shriners Bums Institute, Boston; Tracer Technologies, Somerville, MA: and the School of Medicine, University of Sao Paolo, Ribeirko, Sao Paolo. Brazil. Submitted August 28, 1992; accepted January 8, 1993. Supported by National Institutes of Health Grants No. DK15856, DK42101, and RR88, and by a grant from the Shriners Hospitals for Crtppled Children (15897). J.S.M. was supported by an NIH fellowship (IJiFOSTW904236 and CNPgBR 200535-88.9). Address reprint requests to V. R. Young. Room EI8-613, MIT, Cambridge, MA 02139. Copyright 0 1993 by W.B. Saunders Cornpan) 00260495193/4210-0014$03.0010
PY - 1993/10
Y1 - 1993/10
N2 - The in vivo rate of conversion of phenylalanine to tyrosine (PheOH) can be estimated using combinations of stable isotope-labeled phenylalanine and tyrosine. We have compared in four healthy adult men the rates of phenylalanine conversion to tyrosine based on the following pairs of primed, continuous tracer infusions administered simultaneously: (1) l-[ring-2H5]phenylalanine and 2H2-tyrosine with a 2H4-tyrosine prime, and (2) l-[1-13C]phenylalanine and 2H2-tyrosine with a 1-13C-tyrosine prime. Phenylalanine oxidation was determined from measurement of 13CO2 excretion in expired air. Tracers were given for 8 hours, with subjects being in the postabsorptive state during the first 3 hours and in the fed state during the remaining 5 hours. Mean (±SD) rates (μmol · kg-1 · h-1) of phenylalanine conversion to tyrosine for fasted and fed states, respectively, were 5.1 ± 2.9 and 6.8 ± 3.4 with 2H5-phenylalanine and significantly higher (P < .05) at 11.1 ± 5.6 and 12.7 ± 7.7 with 13C-phenylalanine as tracer. Phenylalanine oxidation was 9.9 ± 2.0 and 13.5 ± 2.6, respectively, for fasted and fed states, and these mean values did not differ (P > .1) from the rate of phenylalanine conversion to tyrosine determined using 13C-phenylalanine. These results indicate the need for caution in interpreting kinetic aspects of phenylalanine metabolism when based on isotopic data from multideuterated phenylalanine. It is suggested that when determinations of rates of phenylalanine conversion to tyrosine based on l-[ring-2H5]phenylalanine are corrected by factors of about 2.2 and 1.8 for fasted and fed states, respectively, they would provide a better estimated of the in vivo rate of conversion of phenylalanine to tyrosine.
AB - The in vivo rate of conversion of phenylalanine to tyrosine (PheOH) can be estimated using combinations of stable isotope-labeled phenylalanine and tyrosine. We have compared in four healthy adult men the rates of phenylalanine conversion to tyrosine based on the following pairs of primed, continuous tracer infusions administered simultaneously: (1) l-[ring-2H5]phenylalanine and 2H2-tyrosine with a 2H4-tyrosine prime, and (2) l-[1-13C]phenylalanine and 2H2-tyrosine with a 1-13C-tyrosine prime. Phenylalanine oxidation was determined from measurement of 13CO2 excretion in expired air. Tracers were given for 8 hours, with subjects being in the postabsorptive state during the first 3 hours and in the fed state during the remaining 5 hours. Mean (±SD) rates (μmol · kg-1 · h-1) of phenylalanine conversion to tyrosine for fasted and fed states, respectively, were 5.1 ± 2.9 and 6.8 ± 3.4 with 2H5-phenylalanine and significantly higher (P < .05) at 11.1 ± 5.6 and 12.7 ± 7.7 with 13C-phenylalanine as tracer. Phenylalanine oxidation was 9.9 ± 2.0 and 13.5 ± 2.6, respectively, for fasted and fed states, and these mean values did not differ (P > .1) from the rate of phenylalanine conversion to tyrosine determined using 13C-phenylalanine. These results indicate the need for caution in interpreting kinetic aspects of phenylalanine metabolism when based on isotopic data from multideuterated phenylalanine. It is suggested that when determinations of rates of phenylalanine conversion to tyrosine based on l-[ring-2H5]phenylalanine are corrected by factors of about 2.2 and 1.8 for fasted and fed states, respectively, they would provide a better estimated of the in vivo rate of conversion of phenylalanine to tyrosine.
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U2 - 10.1016/0026-0495(93)90131-7
DO - 10.1016/0026-0495(93)90131-7
M3 - Article
C2 - 8412744
AN - SCOPUS:0027515159
SN - 0026-0495
VL - 42
SP - 1316
EP - 1322
JO - Metabolism
JF - Metabolism
IS - 10
ER -