AMP deaminase from anterior lobe of bovine pituitary: purification and properties.
Abstract
AMP deaminase (EC 3.5.4.6) from anterior lobe of bovine pituitary has been purified for the first time. Six molecular forms of the enzyme were eluted from phosphocellulose P11 with a KC1 concentration gradient. By two stage gel chromatography individual molecular forms were purified to electrophoretic homogeneity. Comparison of some physico-chemical and kinetic properties of the preparations obtained showed high similarity of their properties to those of AMP deaminase from other animal tissues already described. All the isoforms were found to be Zn(2+)-dependent.Acta Biochimica Polonica is an OpenAccess quarterly and publishes four issues a year. All contents are distributed under the Creative Commons Attribution-ShareAlike 4.0 International (CC BY 4.0) license. Everybody may use the content following terms: Attribution — You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
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