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Solubilization by proteolysis of an activated form of rat liver membrane guanylate cyclase
Author(s) -
Lacombe Marie-Lise,
Haguenauer-Tsapis Rosine,
Stengel Dominique,
Ben Salah Abderraouf,
Hanoune Jacques
Publication year - 1980
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(80)80533-3
Subject(s) - physics , medicine , microbiology and biotechnology , biology
Guanylate cyclase has been found associated with both the supernatant and particulate fractions of almost all animal tissues examined [I-4]. Among the activators of the enzyme described [1,2], none has been clearly proved to be of physiological importance [2]. The membrane-bound guanylate cyclase activity from rat liver was markedly increased by proteolysis [51, while the activity of the cytosolic form remained unchanged or inhibited. Here we report that this proteolytic activation is accompanied, as well, by the solubilization of the enzyme as indicated by its presence in the 165 000 X g supernatant. The adenylate cyclase of the same preparation although activated by proteolysis [6-Sf remains membranebound. The solubilized guanylate cyclase (app. M, -140 000) thus appears as the hydrophilic moiety of the membrane enzyme which can easily be split off from its hydrophobic anchor by proteolysis.