Open AccessCharacterization of an ATPase on the Inside of Rat‐Liver Nuclear Envelopes by Affinity Labeling
Author(s) -
KONDORKOCH Claudia,
RIEDEL Norbert,
VALENTIN Reiner,
FASOLD Hugo,
FISCHER Helmut
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06868.x
Subject(s) - atpase , characterization (materials science) , chemistry , microbiology and biotechnology , biophysics , biochemistry , computational biology , biology , nanotechnology , materials science , enzyme
Nuclear envelope membranes from rat liver cells contain ATPases, one of which can be inhibited and irreversibly labeled by ( S ‐dinitrophenyl)‐6‐mercaptopurine riboside triphosphate. Inhibition and covalent substitution of the ATPase are achieved only after disruption of the nuclei, the ATP analogue is inactive on the ATPase activity of whole nuclei or on vesicles of the membrane prepared after a modified heparin method of Bornens and Courvalin. Electron micrographs and scanning micrographs helped to establish the characterization of closed vesicles and intact nuclei. With the aid of (α‐ 32 P)‐labeled, and of the (β,γ‐ 32 P)‐labeled analogue, it was possible to demonstrate the incorporation of the nucleotide into a few protein regions of the nuclear membrane disc electrophoresis pattern.