Can I read Trypsin Solubilization of Rat Liver Membrane-bound Guanylate Cyclase Results in a Form Kinetically Distinct from the Cytosolic Enzyme. on EtoBox?

Trypsin Solubilization of Rat Liver Membrane-bound Guanylate Cyclase Results in a Form Kinetically Distinct from the Cytosolic Enzyme. by R. Haguenauer-Tsapis; A. Ben Salah; M.L. Lacombe; J. Hanoune is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Trypsin Solubilization of Rat Liver Membrane-bound Guanylate Cyclase Results in a Form Kinetically Distinct from the Cytosolic Enzyme. about?

We have previously reported that treatment of rat liver plasma membranes with various proteases led to activation and solubilization of membrane-bound guanylate cyclase. We report here that the guanylate cyclase solubilized by proteolysis differed from the cytosolic cyclase and rather was similar to the membrane-bound form of the enzyme in that it exhibited a sigmoidal MnGTP concentration dependence and was not activated by an excess Mn2+ or by nitrosocompounds. Also, whereas the cytosolic guanylate cyclase activity was completely abolished by 10 to 100 microM Cd2+, a dithiol reagent, no inhibitory effect was observed on the trypsin-solubilized enzyme. Therefore, the differences in kinetic properties between cytosolic and membrane-bound rat liver guanylate cyclase reside in structural differences between both forms of the enzyme rather than in differences in their environment.

Who reads Trypsin Solubilization of Rat Liver Membrane-bound Guanylate Cyclase Results in a Form Kinetically Distinct from the Cytosolic Enzyme.?

Author

R. Haguenauer-Tsapis; A. Ben Salah; M.L. Lacombe; J. Hanoune

Publisher

Elsevier BV

Published

1981

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)