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Neurochemical Research

, Volume 1, Issue 3, pp 275–298 | Cite as

Brain lysosomal hydrolases: I. Solubilization and electrophoretic behavior of acid hydrolases in nerve-ending and mitochondrial-lysosomal fractions from rat brain. Effects of autolysis, neuraminidase, and storage

  • Abdussamad Patel
  • Harold Koenig
Article

Abstract

In solubility studies of 7 acid hydrolases, the extent of solubilization by sonic disruption varied with the enzyme species and increased with increasing pH and Triton X-100 concentration of the suspension medium. Hydrolases in the nerve-ending (NE) fraction were more resistant to solubilization than those in the mitochondrial-lysosomal (M-L) fraction, but nearly quantitative solubilization was attained by sonication in an alkaline buffer containing 0,5% Triton X-100. Polyacrylamide gel electrophoresis of extracts revealed multiple components of acid phosphatase, acid esterase, arylsulfatase,β-glucuronidase, andβ-N-acetyl-hexosaminidase. The enzyme patterns varied with the subcellular fraction and the composition of the medium. In general, the acidic (anodic) forms of these hydrolases were more readily solubilized by sonication in acidic buffer, alkaline pH and Triton X-100 being required to solubilize the basic (cationic) components. The acidic forms of these enzymes were converted to less anodic or cathodic forms, or both, during autolysis at pH 6 at 0 and 37°C, and during storage at −20°C.

Keywords

Acid Phosphatase Subcellular Fraction Acidic Buffer Multiple Component Solubility Study 
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.

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Copyright information

© Plenum Publishing Corporation 1976

Authors and Affiliations

  • Abdussamad Patel
    • 1
    • 2
  • Harold Koenig
    • 1
    • 2
  1. 1.Neurology ServiceVeterans Administration Lakeside HospitalChicago
  2. 2.Department of NeurologyNorthwestern University Medical SchoolChicago

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