Affinity Chromatography on Heparin-Sepharose of Rat Adipose Tissue Triglyceride Lipase from Cytosol

  • A. Vanhove
  • M. Breton
  • J. Polonovski
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 101)


Subfractionation of the fat free homogenate of rat adipose tissue showed that a high yield of triglyceride lipase was recovered reproducibly in the microsomal supernatant fraction (cytosol) when rat epididymal fat pads were homogenized in sucrose-EDTA-Tris medium.

Triglyceride lipase was bound on heparin-Sepharose. Hydrolyzing activity towards triacylglycerol was eluted as a single, sharp peak in 0.7 M NaCl, 5 mM sodium barbital and 20 % glycerol (pH 7.0). The triglyceride lipase was not inhibited by 1 M NaC1 and not sti­mulated by the presence of fresh human serum.

A lipoprotein-lipase activity was demonstrable in the cytosol when adipose tissue from fed rats were used. Fasting of the animals lowered this activity.


Lipase Activity Cyanogen Bromide Triglyceride Lipase Triacylglycerol Lipase Sodium Barbital 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Khoo, J.C., Jarett, L., Mayer, S.E. and Steinberg, D. (1972) J. Biol. Chem. 247, 4812.PubMedGoogle Scholar
  2. 2.
    Huttunen, J.K., Ellingboe, J., Pittman, R.C. and Steinberg, D.(1970)Biochim. Biophys. Acta. 218, 333.CrossRefGoogle Scholar
  3. 3.
    Korn, E.D. and Quigley, T.W. (1957) J. Biol. Chem. 226, 833.PubMedGoogle Scholar
  4. 4.
    Mc Keel, D.W. and Jarett, L. (1970) J. Cell. Biol. 44, 417.CrossRefGoogle Scholar
  5. 5.
    Dole, V.P. (1956) J. Clin. Invest. 35, 160.CrossRefGoogle Scholar
  6. 6.
    Kelley, T.F. (1968) J. Lipid. Res. 9, 799.PubMedGoogle Scholar
  7. 7.
    Dixon, T.F. and Purdom, M. (1954) J. Clin. Path. 7, 341.PubMedCrossRefGoogle Scholar
  8. 8.
    Mackler, B. (1967) Methods in enzymology, vol. X, 551, Ed. R.W. Estabrook and M.E. Pullman.Google Scholar
  9. 9.
    Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) J. Biol. Chem. 193, 265.PubMedGoogle Scholar
  10. 10.
    Iverius, P.M. (1971) Biochem. J. 124, 677.PubMedGoogle Scholar
  11. 11.
    Wolf, C., Vanhove, A., Breton, M., Etienne, J., Béréziat, G. and Polonovski, J. (1975) C. R. Soc. Biol. 169, 1145.Google Scholar
  12. 12.
    Matsumura, S., Matsuo, M. and Nishizuka, Y. (1976) J. Biol. Chem. 251, 6267.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • A. Vanhove
    • 1
  • M. Breton
    • 1
  • J. Polonovski
    • 1
  1. 1.Department of BiochemistryU.E.R. Saint-Antoine 27Paris Cédex 12France

Personalised recommendations