Circular dichroism changes in galactosyltransferase upon substrate binding;.

C R Geren; S C Magee; K E Ebner

doi:10.1021/bi00678a017

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Circular dichroism changes in galactosyltransferase upon substrate binding;.

C R Geren·S C Magee·K E Ebner

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Abstract

Circular dichroism studies with the galactosyltransferase isolated from bovine skim milk are described. Addition of UDP-galactose to the galactosyltransferase-Mn-2+ complex causes a decrease in the negative mean residue ellipticity in the 205-220-nm range and positive increases in the 265- and 275-290-nm ellipticity. These date are consistent with the view that a conformation change involving aromatic amino acid residues occurs upon the binding of UDP-galactose to the galactosyltransferase-Mn-2+ complex. No effects in the near-ultraviolet circular dichroism spectrum were observed upon the addition of UDP or glucose to the galactosyltransferase-Mn-2+ complex.

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Animals Binding Sites Cattle Circular Dichroism Female Galactose Hexosyltransferases Kinetics Manganese Milk Protein Binding Protein Conformation Spectrophotometry, Ultraviolet Uridine Diphosphate Sugars Journal Article Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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C R Geren, S C Magee, K E Ebner. 1975-04-08. Circular dichroism changes in galactosyltransferase upon substrate binding;.. https://doi.org/10.1021/bi00678a017

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