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Identical catalytic subunit in both molecular forms of hormone‐sensitive cholesterol esterase from bovine adrenal cortex
Author(s) -
Sonnenborn Ulrich,
Eiteljörge Günter,
Trzeciak Wieslaw H.,
Kunau Wolf-H.
Publication year - 1982
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(82)80181-6
Subject(s) - library science , computer science
The activity of neutral cholesterol esterase (sterol-ester acylhydrolase, EC 3.1.1.13) in the adrenal gland is enhanced by stress [ 1,2] or by administration of ACTH [3-51. This increase of enzymatic activity is supposed to be due to phosphorylation of the enzyme by CAMP-dependent protein kinase [6-91; for review see [lo]. Therefore, since hormone-sensitive cholesterol esterase has not been purified to apparent homogeneity or characterized in molecular terms, it has been impossible to provide direct evidence for the proposed covalent modification of the enzyme.