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Biochemical studies of a human low-activity galactose-1-phosphate uridyl transferase variant.
J Inherit Metab Dis. 1978; 1(4):145-51.JI

Abstract

A low activity galactose-1-phosphate uridyl transferase (transferase) variant in a newborn infant has been demonstrated by biochemical studies in erythrocytes and cultured skin fibroblasts. The newborn infant was a galactosaemic suspect identified in a neonatal metabolic screening programme. On breast feeding, he did well without clinical symptoms of galactosaemia during the first 15 days of life. However, substantial amounts of erythrocyte galactose-1-phosphate and urinary galactitol corresponding to the levels in untreated galactosaemic patients, along with mild amino aciduria, were found. The transferase activity, as measured by a sensitive micro kinetic radioisotopic method, was about 7--10% of the normal. On starch gel electrophoresis, the enzyme from the haemolysate had similar mobility as the normal in Tris--glycine buffer, pH 8.8 and phosphate buffer, pH 7.0, but had a slower mobility than that of the normal in the histidine buffer, pH 7.8. The mobility difference was much clearer in a semipurified enzyme preparation. The transferase enzyme in the haemolysate appeared to be more heat labile.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Case Reports
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

117249

Citation

Ng, W G., et al. "Biochemical Studies of a Human Low-activity Galactose-1-phosphate Uridyl Transferase Variant." Journal of Inherited Metabolic Disease, vol. 1, no. 4, 1978, pp. 145-51.
Ng WG, Kline F, Lin J, et al. Biochemical studies of a human low-activity galactose-1-phosphate uridyl transferase variant. J Inherit Metab Dis. 1978;1(4):145-51.
Ng, W. G., Kline, F., Lin, J., Koch, R., & Donnell, G. N. (1978). Biochemical studies of a human low-activity galactose-1-phosphate uridyl transferase variant. Journal of Inherited Metabolic Disease, 1(4), 145-51.
Ng WG, et al. Biochemical Studies of a Human Low-activity Galactose-1-phosphate Uridyl Transferase Variant. J Inherit Metab Dis. 1978;1(4):145-51. PubMed PMID: 117249.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biochemical studies of a human low-activity galactose-1-phosphate uridyl transferase variant. AU - Ng,W G, AU - Kline,F, AU - Lin,J, AU - Koch,R, AU - Donnell,G N, PY - 1978/1/1/pubmed PY - 1978/1/1/medline PY - 1978/1/1/entrez SP - 145 EP - 51 JF - Journal of inherited metabolic disease JO - J. Inherit. Metab. Dis. VL - 1 IS - 4 N2 - A low activity galactose-1-phosphate uridyl transferase (transferase) variant in a newborn infant has been demonstrated by biochemical studies in erythrocytes and cultured skin fibroblasts. The newborn infant was a galactosaemic suspect identified in a neonatal metabolic screening programme. On breast feeding, he did well without clinical symptoms of galactosaemia during the first 15 days of life. However, substantial amounts of erythrocyte galactose-1-phosphate and urinary galactitol corresponding to the levels in untreated galactosaemic patients, along with mild amino aciduria, were found. The transferase activity, as measured by a sensitive micro kinetic radioisotopic method, was about 7--10% of the normal. On starch gel electrophoresis, the enzyme from the haemolysate had similar mobility as the normal in Tris--glycine buffer, pH 8.8 and phosphate buffer, pH 7.0, but had a slower mobility than that of the normal in the histidine buffer, pH 7.8. The mobility difference was much clearer in a semipurified enzyme preparation. The transferase enzyme in the haemolysate appeared to be more heat labile. SN - 0141-8955 UR - https://www.unboundmedicine.com/medline/citation/117249/Biochemical_studies_of_a_human_low_activity_galactose_1_phosphate_uridyl_transferase_variant_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0141-8955&date=1978&volume=1&issue=4&spage=145 DB - PRIME DP - Unbound Medicine ER -