Purification and some properties of ATP-citrate lyase from rat brain

Andrzej Szutowicz, P. Srere

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

ATP-citrate lyase has been purified from rat brain by a new procedure which yields an enzyme of specific activity of 21 U/mg protein (37 °C) (2050-fold purification). Purity (by sodium dodecyl sulfate-gel electrophoresis) of the preparation was comparable to that of rat liver ATP-citrate lyase of similar specific activity. Both brain and liver ATP-citrate lyase have the same electrophoretic mobility, as well as the same immunoreactivity against specific rabbit anti-rat liver ATP-citrate lyase antibody. These data indicate that rat brain ATP-citrate lyase is similar or identical to that present in rat liver. Intraperitoneally injected 32Pi was incorporated into the structural phosphate of ATP-citrate lyase in rat liver but not into the rat brain enzyme.

Original languageEnglish
Pages (from-to)168-174
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume221
Issue number1
DOIs
Publication statusPublished - Feb 15 1983

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ATP Citrate (pro-S)-Lyase
Purification
Rats
Brain
Liver
Electrophoretic mobility
Enzymes
Protein C
Electrophoresis
Sodium Dodecyl Sulfate
Gels
Phosphates
Rabbits
Antibodies

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Purification and some properties of ATP-citrate lyase from rat brain. / Szutowicz, Andrzej; Srere, P.

In: Archives of Biochemistry and Biophysics, Vol. 221, No. 1, 15.02.1983, p. 168-174.

Research output: Contribution to journalArticle

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