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Subcellular Localization of Angiotensin‐Converting Enzyme in Cultured Neuroblastoma Cells
Author(s) -
Clemens D. L.,
Okamura T.,
Inagami T.
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb13096.x
Subject(s) - membrane , enzyme , proteases , cell fractionation , differential centrifugation , chemistry , substrate (aquarium) , centrifugation , density gradient , biochemistry , angiotensin ii , biophysics , chromatography , biology , receptor , ecology , physics , quantum mechanics
Angiotensin‐converting enzyme (ACE) activity of Neuro‐2A mouse neurobiastoma cells was found predominantly in particulate fractions. Density gradient centrifugation of the particulate fractions showed ACE activity in light fractions of the gradient, a result suggesting a plasma membrane localization. This was confirmed using the aqueous two‐phase polymer system of plasma membrane isolation. The rapid and energy‐independent hydrolysis of exogenous substrate by ACE of intact cells and the sensitivity of the enzyme of intact cells to proteases indicate further that the active site of ACE is oriented extracellularly.