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Purification of normal and inactive galactosemic galactose-1-phosphate uridylyltransferase from human red cells.
J Biol Chem. 1976 Feb 25; 251(4):1057-63.JB

Abstract

A rapid method is described for the purification of galactose-1-phosphate uridylyltransferase (EC 2.7.7.12) from human red blood cells by the use of DEAE-cellulose and two steps of affinity chromatography on a "uridine-aminohexyl" agarose column. The enzyme consists of two identical subunits of 31,000 molecular weight as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Chromatography on Sephadex G-200 chromatography gave a molecular weight of 69,000 for the native enzyme, it being eluted from the column with bovine serum albumin. Cross-linking of the enzyme with dimethylsuberimidate followed by analysis of the products by sodium dodecyl sulfate polyacrylamide gel electrophoresis caused the near-disappearance of the 31,000 molecular weight subunit and the appearance of a protein with a molecular weight of about 65,000 without the appearance of higher polymers.

Authors

No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

814122

Citation

Dale, G L., and G Popják. "Purification of Normal and Inactive Galactosemic Galactose-1-phosphate Uridylyltransferase From Human Red Cells." The Journal of Biological Chemistry, vol. 251, no. 4, 1976, pp. 1057-63.
Dale GL, Popják G. Purification of normal and inactive galactosemic galactose-1-phosphate uridylyltransferase from human red cells. J Biol Chem. 1976;251(4):1057-63.
Dale, G. L., & Popják, G. (1976). Purification of normal and inactive galactosemic galactose-1-phosphate uridylyltransferase from human red cells. The Journal of Biological Chemistry, 251(4), 1057-63.
Dale GL, Popják G. Purification of Normal and Inactive Galactosemic Galactose-1-phosphate Uridylyltransferase From Human Red Cells. J Biol Chem. 1976 Feb 25;251(4):1057-63. PubMed PMID: 814122.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification of normal and inactive galactosemic galactose-1-phosphate uridylyltransferase from human red cells. AU - Dale,G L, AU - Popják,G, PY - 1976/2/25/pubmed PY - 1976/2/25/medline PY - 1976/2/25/entrez SP - 1057 EP - 63 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 251 IS - 4 N2 - A rapid method is described for the purification of galactose-1-phosphate uridylyltransferase (EC 2.7.7.12) from human red blood cells by the use of DEAE-cellulose and two steps of affinity chromatography on a "uridine-aminohexyl" agarose column. The enzyme consists of two identical subunits of 31,000 molecular weight as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Chromatography on Sephadex G-200 chromatography gave a molecular weight of 69,000 for the native enzyme, it being eluted from the column with bovine serum albumin. Cross-linking of the enzyme with dimethylsuberimidate followed by analysis of the products by sodium dodecyl sulfate polyacrylamide gel electrophoresis caused the near-disappearance of the 31,000 molecular weight subunit and the appearance of a protein with a molecular weight of about 65,000 without the appearance of higher polymers. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/814122/Purification_of_normal_and_inactive_galactosemic_galactose_1_phosphate_uridylyltransferase_from_human_red_cells_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=814122 DB - PRIME DP - Unbound Medicine ER -