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Bromobimane crosslinking studies in oligomycin‐sensitive ATPase from beef heart mitochondria
Author(s) -
Zimmer Guido,
Mainka Luise,
Heil Berthold M.
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)81335-5
Subject(s) - oligomycin , mitochondrion , reagent , atpase , chemistry , fluorescence , biochemistry , biophysics , enzyme , biology , physics , quantum mechanics
Using a bromobimane fluorescent label the M r 31 000 protein band oligomycin‐sensitive (OS)‐ATPase from beef heart mitochondria is shown to become much intensified by 2‐mercaptopropionylglycine. In the presence of 3.5 nmol/mg protein of the thiol reagent ATP—P i exchange activity is increased by 90%. With the fluorescent crosslinking reagent dibromobimane (DB) we show that a new fluorescent peak appears between M r 50 000 and 60 000. ATP—P i exchange is very much decreased by DB. The results suggest that for regulation of ATP‐synthetase activity sulfhydryl groups in the region of the M r 31 000 protein(s) play an important role.