Butyrate-Binding Protein from Rat and Mouse Liver1
- 1 February 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 83 (2) , 349-356
- https://doi.org/10.1093/oxfordjournals.jbchem.a131920
Abstract
A novel component which specifically binds butyrate was found in rat and mouse liver. This component, termed butyrate protein (BBP), is localized in the cytosolic fraction and exhibits protein charcteristics, such as heat-and protease-sensitivity. The size of BBP was found to be 7.6S,while it was converted to subunits of 45,000–48,000 dalton by treatment with sodium dodecyl sulfate. The dissociation constant of the binding of BBP with butyrate was 2.22×10−5 M in the standard assay. 30-Fold purification of BBP was achived by batch wise adsorption and elution from CM-cellulose and hydroxylapatite column chromatography. BBP is clearly distinguishable from the fatty acid-binding protein found previously on the basis of its size and binding specificity.This publication has 3 references indexed in Scilit:
- Fatty acid binding to cytoplasmic proteins of myocardium and red and white skeletal muscle in the rat. A possible new role for myoglobinBiochemical and Biophysical Research Communications, 1977
- Induction by short‐chain fatty acids of alkaline phosphatase activity in cultured mammalian cellsJournal of Cellular Physiology, 1976
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934