Neurochemical Research

, Volume 8, Issue 10, pp 1285–1293 | Cite as

Degradation of myelin basic protein by calcium-activated neutral protease (CANP) in human brain and inhibition by E-64 analogue

  • Katsuhiko Yanagisawa
  • Shuzo Sato
  • Nobutada Amaya
  • Tadashi Miyatake
Original Articles


A calcium-activated neutral protease (CANP) was extracted from human brain and partially purified. The activity was measured using alkali-denatured casein (Hammersten) as a substrate. The optimum pH was around 7.0. The activity required the presence of calcium ions, maximum activity was obtained with over 5 mM calcium ions. TheKm for the casein concentration was about 1.62 mg/ml. The activity of CANP was inhibited by one of the thiol protease inhibitors, E-64 analogue (E-64-a). The rate of inhibition was about 50% at an E-64-a concentration of 10−5M. This CANP degraded selectively basic protein in myelin proteins and the degradation was inhibited by E-64-a or EGTA. The role of the brain CANP in the process of demyelination was suggested by this study.


Calcium Protease Inhibitor Thiol Human Brain EGTA 


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Copyright information

© Plenum Publishing Corporation 1983

Authors and Affiliations

  • Katsuhiko Yanagisawa
    • 1
  • Shuzo Sato
    • 1
  • Nobutada Amaya
    • 1
  • Tadashi Miyatake
    • 1
  1. 1.Department of Neurology Brain Research InstituteNiigata UniversityNiigataJapan

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