TY - JOUR
T1 - Methylthioadenosine phosphorylase activity in human erythrocytes
AU - Sahota, Amrik
AU - Webster, Dianne R.
AU - Potter, Catherine F.
AU - Simmonds, H. Anne
AU - Rodgers, A. Victoria
AU - Gibson, Terence
N1 - Funding Information:
This work was supported by Grants from the Medical Research Council, the Arthritis and Rheumatism Council, The Nuffield Foundation and the Wellcome Trust.
PY - 1983/3/14
Y1 - 1983/3/14
N2 - An enzyme capable of degrading 5'-methylthioadenosine to adenine was found in the human erythrocyte. A rapid assay for this enzyme, 5'-methylthioadenosine phosphorylase, was developed using high pressure liquid chromatography. The specific activity in 24 normal subjects was 8.9 ± 2.0 nmol · mg-1 Hb · h-1. Levels within this range were also found in erythrocyte lysates from gouty subjects and patients with a variety of inborn errors of purine metabolism, including patients with a complete deficiency of the adenine salvage enzyme - adenine phosphoribosyltransferase. Erythrocyte lysates from the latter however, were unable to convert the adenine produced to AMP in a linked assay system, in contrast to controls and other patients. These results support the suggestion that adenine, which is excreted in quantity by patients with adenine phosphoribosyltransferase deficiency is derived endogenously from 5'-methylthioadenosine as a by-product of polyamine biosynthesis.
AB - An enzyme capable of degrading 5'-methylthioadenosine to adenine was found in the human erythrocyte. A rapid assay for this enzyme, 5'-methylthioadenosine phosphorylase, was developed using high pressure liquid chromatography. The specific activity in 24 normal subjects was 8.9 ± 2.0 nmol · mg-1 Hb · h-1. Levels within this range were also found in erythrocyte lysates from gouty subjects and patients with a variety of inborn errors of purine metabolism, including patients with a complete deficiency of the adenine salvage enzyme - adenine phosphoribosyltransferase. Erythrocyte lysates from the latter however, were unable to convert the adenine produced to AMP in a linked assay system, in contrast to controls and other patients. These results support the suggestion that adenine, which is excreted in quantity by patients with adenine phosphoribosyltransferase deficiency is derived endogenously from 5'-methylthioadenosine as a by-product of polyamine biosynthesis.
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U2 - 10.1016/0009-8981(83)90328-5
DO - 10.1016/0009-8981(83)90328-5
M3 - Article
C2 - 6406103
AN - SCOPUS:0020535317
SN - 0009-8981
VL - 128
SP - 283
EP - 290
JO - Clinica Chimica Acta
JF - Clinica Chimica Acta
IS - 2-3
ER -