The partial purification and comparative analysis of serine transhydroxymethylase from bovine liver and brain
Serine transhydroxymethylase has been purified one hundred fold from bovine liver and brain. The enzyme preparation obtained from either tissue showed one major band containing 75% of the protein and one minor band when analyzed by polyacrylamide gel electrophoresis. Several properties of the two enzymes were studied. The enzyme from liver was able to undergo a heat step resulting in increased activity while that from brain was denatured under the same conditions. The liver enzyme was found to be fifty times as active as that of brain and the former showed a constant ratio of serine transhydroxymethylase activity to threonine aldolase activity during purification while the latter lost all ability to convert threonine to acetaldehyde. The Rf values for the major component on polyacrylamide gels were 0.06 for liver and 0.4 for brain. Gel filtration showed the liver enzyme to have a molecular weight of approximately 200,000 and the brain enzyme a molecular weight of 140,000 while polyacrylamide gel electrophoresis in SDS showed subunit molecular weight values for the major bands of 48,000 for the liver and 28,000 for the brain enzyme.
College and Department
Physical and Mathematical Sciences; Chemistry and Biochemistry
BYU ScholarsArchive Citation
Turpin, Kathleen Candland, "The partial purification and comparative analysis of serine transhydroxymethylase from bovine liver and brain" (1973). Theses and Dissertations. 8372.
Enzymes, Liver, Brain, Cattle