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Galactose-1-phosphate uridyl transferase in fibroblasts: isozymes in normal and variant states.
Ann Hum Genet. 1975 Oct; 39(2):147-50.AH

Abstract

Electorphoretic properties of galactose-1-phosphate uridyl transferase in cultured skin fibroblasts of normal humans and individuals with different enzyme variants have been studied. Normal fibroblast lysates showed four activity bands, each slower moving than the erythrocyte enzyme. The transferase variants revealed different mobilities analogous to those found in erythrocytes. These findings suggest that subunits of human transferase associate variously with one another in a manner specific for each tissue and that in transferase variant states, an altered subunit results in a characteristic alteration in electrophoretic mobility which is analogous for each tissue.

Authors

Hammersen G
No affiliation info available
Mandell R
No affiliation info available
Levy HL
No affiliation info available

MeSH

Electrophoresis, Starch GelFibroblastsGalactoseGalactosemiasGenetic VariationHumansNucleotidyltransferasesSkinUTP-Hexose-1-Phosphate Uridylyltransferase

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

1052762

Citation

Hammersen, G, et al. "Galactose-1-phosphate Uridyl Transferase in Fibroblasts: Isozymes in Normal and Variant States." Annals of Human Genetics, vol. 39, no. 2, 1975, pp. 147-50.
Hammersen G, Mandell R, Levy HL. Galactose-1-phosphate uridyl transferase in fibroblasts: isozymes in normal and variant states. Ann Hum Genet. 1975;39(2):147-50.
Hammersen, G., Mandell, R., & Levy, H. L. (1975). Galactose-1-phosphate uridyl transferase in fibroblasts: isozymes in normal and variant states. Annals of Human Genetics, 39(2), 147-50.
Hammersen G, Mandell R, Levy HL. Galactose-1-phosphate Uridyl Transferase in Fibroblasts: Isozymes in Normal and Variant States. Ann Hum Genet. 1975;39(2):147-50. PubMed PMID: 1052762.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Galactose-1-phosphate uridyl transferase in fibroblasts: isozymes in normal and variant states. AU - Hammersen,G, AU - Mandell,R, AU - Levy,H L, PY - 1975/10/1/pubmed PY - 1975/10/1/medline PY - 1975/10/1/entrez SP - 147 EP - 50 JF - Annals of human genetics JO - Ann Hum Genet VL - 39 IS - 2 N2 - Electorphoretic properties of galactose-1-phosphate uridyl transferase in cultured skin fibroblasts of normal humans and individuals with different enzyme variants have been studied. Normal fibroblast lysates showed four activity bands, each slower moving than the erythrocyte enzyme. The transferase variants revealed different mobilities analogous to those found in erythrocytes. These findings suggest that subunits of human transferase associate variously with one another in a manner specific for each tissue and that in transferase variant states, an altered subunit results in a characteristic alteration in electrophoretic mobility which is analogous for each tissue. SN - 0003-4800 UR - https://www.unboundmedicine.com/medline/citation/1052762/Galactose_1_phosphate_uridyl_transferase_in_fibroblasts:_isozymes_in_normal_and_variant_states_ DB - PRIME DP - Unbound Medicine ER -