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Heterogeneity of three electrophoretically distinct G o α‐subunits in mammalian brain
Author(s) -
Spicher Karsten,
Nuernberg Bernd,
Jäger Babette,
Rosenthal Walter,
Schultz Günter
Publication year - 1992
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(92)80770-h
Subject(s) - protein subunit , gene isoform , biology , microbiology and biotechnology , membrane , cloning (programming) , electrophoresis , alternative splicing , gel electrophoresis , biochemistry , gene , chemistry , computer science , programming language
So far three splice variants of the α o ‐gene coding for two α o proteins have been identified by molecular cloning, and the corresponding proteins purified. In the present study subtype‐specific peptide antibodies revealed the existence of an electrophoretically distinct third form of α o in mammalian brain membranes which migrates more slowly on SDS‐PAGE and shows a more acidic pI value than the other α o ‐subunits. Each of the three α o ‐subunits is detected as two isoforms when enriched from brain membranes. Rodent α o ‐subunits differ from non‐rodent species in their electrophoretic mobilities. The results suggest that (i) there may exist a novel α o ‐subunit which reacts with an α o ‐subunit‐specific antibody, (ii) each α o ‐subunit may exist in more than one co‐ or posttranslationally modified isoform in brain membranes, and (iii) differences between α o ‐subunits from different species exist which are detectable by gel electrophoretic methods.