Multiple Chromatographic Forms of ATP Citrate Lyase from Rat Liver

Overview

Journal Biochem J

Specialty Biochemistry

Date 1983 Aug 15

PMID 6615476

Citations 1

Authors

A P Corrigan

C C Rider

Affiliations

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Abstract

ATP citrate lyase is shown to exist as multiple forms in extracts of rat liver. DEAE-Sephadex ion-exchange chromatography of liver supernatants reveals two peaks of activity. A minor, basic, component, comprising 14% of the recovered activity, is eluted without retention, whereas the major, acidic, form is eluted by a KCl gradient. Gel filtration of similar extracts shows the presence of a high-Mr form of ATP citrate lyase (Mr around 10(7) in addition to the tetrameric enzyme (Mr 4.1 X 10(5). This associated state, which represents 10% of the total activity, is unstable, breaking down to the tetramer, and appears to be disrupted by Mg2+. The basic form changes in the partially purified state to give the acidic form. Most of the high-Mr enzyme is acidic in nature. No evidence could be found for an association of the enzyme with mitochondrial or microsomal membranes. ATP citrate lyase from rat brain also shows two peaks of activity on DEAE-Sephadex ion-exchange chromatography, but the activity is distributed between the peaks in almost equal proportions. However, only the tetrameric enzyme was observed on gel filtration.

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References

Sottocasa G, Kuylenstierna B, Ernster L, Bergstrand A . An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study. J Cell Biol. 1967; 32(2):415-38. PMC: 2107253. DOI: 10.1083/jcb.32.2.415. View

SRERE P . The citrate cleavage enzyme. I. Distribution and purification. J Biol Chem. 1959; 234:2544-7. View

Rose I, WARMS J . Mitochondrial hexokinase. Release, rebinding, and location. J Biol Chem. 1967; 242(7):1635-45. View

Suzuki F, Fukunishi K, Daikuhara Y, Takeda Y . Studies on ATP citrate lyase of rat liver. II. Immunochemical properties. J Biochem. 1967; 62(2):170-8. DOI: 10.1093/oxfordjournals.jbchem.a128645. View

Daikuhara Y, Tsunemi T, Takeda Y . The role of ATP citrate lyase in the transfer of acetyl groups in rat liver. Biochim Biophys Acta. 1968; 158(1):51-61. DOI: 10.1016/0304-4165(68)90071-8. View

Cottam G, SRERE P . The sulfhydryl groups of citrate cleavage enzyme. Arch Biochem Biophys. 1969; 130(1):304-11. DOI: 10.1016/0003-9861(69)90037-x. View

Watson J, Lowenstein J . Citrate and the conversion of carbohydrate into fat. Fatty acid synthesis by a combination of cytoplasm and mitochondria. J Biol Chem. 1970; 245(22):5993-6002. View

Smoly J, Wakabayashi T, ADDINK A, Green D . Partial purification of the outer membrane fraction from sonicated heavy beef heart mitochondria. Arch Biochem Biophys. 1971; 143(1):6-21. DOI: 10.1016/0003-9861(71)90181-0. View

Szutowicz A, Stepien M, Angielski S . The inhibition of rat brain ATP: citrate oxaloacetate-lyase by L-glutamate. J Neurochem. 1974; 22(1):85-91. DOI: 10.1111/j.1471-4159.1974.tb12182.x. View

10.

Lane M, Moss J, Polakis S . Acetyl coenzyme A carboxylase. Curr Top Cell Regul. 1974; 8(0):139-95. View

11.

Inoue H, Lowenstein J . Acetyl coenzyme A carboxylase from rat liver. EC 6.4.1.2 acetyl-CoA: carbon dioxide ligase (ADP). Methods Enzymol. 1975; 35:3-11. DOI: 10.1016/0076-6879(75)35131-8. View

12.

Singh M, RICHARDS E, Mukherjee A, SRERE P . Structure of ATP citrate lyase from rat liver. Physicochemical studies and proteolytic modification. J Biol Chem. 1976; 251(17):5242-50. View

13.

Linn T, SRERE P . Identification of ATP citrate lyase as a phosphoprotein. J Biol Chem. 1979; 254(5):1691-8. View

14.

Alexander M, Kowaloff E, Witters L, Dennihy D, Avruch J . Purification of a hepatic 123,000-dalton hormone-stimulated 32P-peptide and its identification as ATP-citrate lyase. J Biol Chem. 1979; 254(16):8052-6. View

15.

Ramakrishna S, Benjamin W . Fat cell protein phosphorylation. Identification of phosphoprotein-2 as ATP-citrate lyase. J Biol Chem. 1979; 254(18):9232-6. View

16.

Janski A, SRERE P, Cornell N, Veech R . Phosphorylation of ATP citrate lyase in response to glucagon. J Biol Chem. 1979; 254(19):9365-8. View

17.

Hoffmann G, Schiessl J, WEISS L . ATP citrate (pro-3S)-lyase in the rat; two-step purification procedure, properties, organ distribution. Hoppe Seylers Z Physiol Chem. 1979; 360(10):1445-51. DOI: 10.1515/bchm2.1979.360.2.1445. View

18.

Guy P, Cohen P, Hardie D . Rat mammary gland ATP-citrate lyase is phosphorylated by cyclic amp-dependent protein kinase. FEBS Lett. 1980; 109(2):205-8. DOI: 10.1016/0014-5793(80)81087-8. View

19.

Janski A, Cornell N . Association of ATP citrate lyase with mitochondria. Biochem Biophys Res Commun. 1980; 92(1):305-12. DOI: 10.1016/0006-291x(80)91553-3. View

20.

Janski A, Cornell N . Subcellular distribution of enzymes determined by rapid digitonin fractionation of isolated hepatocytes. Biochem J. 1980; 186(2):423-9. PMC: 1161592. DOI: 10.1042/bj1860423. View