Bulletin of Experimental Biology and Medicine

, Volume 80, Issue 4, pp 1179–1180 | Cite as

Molecular forms of acid brain proteinases

  • L. M. Stepchenko
  • V. A. Berezin
  • A. D. Reva
  • A. I. Yalovoi
Biochemistry and Biophysics
  • 13 Downloads

Abstract

Acid proteinases of the brain were isolated by gel filtration on a column with Sephadex G-100. Three peaks of enzyme activity were found. Cathepsin D with high molecular weight (over 150,000) is solubilized from brain tissues by 0.1% Triton X-100. Cathepsin D with a molecular weight of 59,000 is solubilized only by a 0.2% solution of the detergent. Low-molecular-weight (20,000) cathepsin D is a soluble cytoplasmic enzyme. The results are regarded as proof of the heterogeneity of molecular forms of acid proteinases in the cerebral cortex, corresponding to the strength of the bond between the enzymes and subcellular structure of brain tissue.

Key Words

brain acid proteinases fractionation cathepsin D molecular forms 

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Copyright information

© Plenum Publishing Corporation 1976

Authors and Affiliations

  • L. M. Stepchenko
  • V. A. Berezin
  • A. D. Reva
  • A. I. Yalovoi

There are no affiliations available

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