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- W1436238093 abstract "This chapter focuses on the enzymes of the leloir pathway, and describes the quantitative determination of enzymatic activity in broken cell preparations. Specific enzymatic assays designed especially for use with crude bacterial extracts are described. Galactokinase catalyzes the reaction ATP + Gal→ ADP +α -Gal-l-P. The Gal-1-P produced in a preincubation mixture is quantitatively determined. The Gal-l-P formed is determined in the proteinfree filtrate by an analytical incubation mixture. The absolute molar amount of TPNH formed is a direct measure of Gal-l-P and is thus a measure of galacto-kinase activity. The rate of G-1-P formation in Gal-l-P uridyl transferase is analyzed by adding the two indicator enzymes and coenzymes in excess, phosphoglueomutase (plus glucose-l,6-diphosphate) and G-6-P dehydrogenase plus TPN. In UDPGal-4-epimerase, UDPG formed is determined in a protein-free filtrate by means of a DPN-dependent specific dehydrogenase (UDPG dehydrogenase). The chapter also describes the purification of galactose-l-phosphate uridyl transferase, and purification of UDPgalactose-4-epimerase." @default.
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- W1436238093 date "1962-01-01" @default.
- W1436238093 modified "2023-10-11" @default.
- W1436238093 title "[20] Enzymes of the Leloir pathway" @default.
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- W1436238093 doi "https://doi.org/10.1016/s0076-6879(62)05204-0" @default.
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