Neurochemical Research

, Volume 21, Issue 4, pp 457–462 | Cite as

Characterization of guanylyl cyclase in purified myelin

  • Michael Grabow
  • Goutam Chakraborty
  • Robert W. Ledeen
Original Articles


This study was undertaken to characterize the enzymatic properties of the particulate guanylyl cyclase previously shown to be present at a high level of activity in purified rat brain myelin. Significant activation was achieved by both Lubrol-PX and Triton X-100, the latters being somewhat more effective. A pH optimum of 7.8 was observed, compared to 7.4 for microsomes. Employing 1.2 mM GTP with 1% Triton X-100, linearity of response was observed up to 60 min and approximately 1.2 mg of myelin protein. Kinetic analysis revealed Km values of 0.258 mM and 0.486mM for myelin and microsomes, respectively, similar values being obtained by Lineweaver-Burke analysis or Direct Linear Plot. Vmax values were 20 and 266 pmol/mg protein/min for myelin and microsomes, respectively. Washing of the myelin with 0.5 M NaCl or 0.1% Na taurocholate did not remove a significant amount of guanylyl cyclase activity, indicating the enzyme to be intrinsic to the myelin sheath.

Key words

Myelin guanylyl cyclase myelin intrinsic enzymes 



guanylyl cyclase




phenylmethylsulfonyl fluoride


2-(N-morpholino)-ethanesulfonic acid




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Copyright information

© Plenum Publishing Corporation 1996

Authors and Affiliations

  • Michael Grabow
    • 1
  • Goutam Chakraborty
    • 1
  • Robert W. Ledeen
    • 1
  1. 1.Department of Neurosciences, New Jersey Medical SchoolUMDNJNewark

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