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Benzylaminopurine‐induced coupling between calmodulin and Ca‐ATPase in wheat root microsomal membranes
Author(s) -
Oláh Zoltán,
Bérczi Alajos,
Erdei László
Publication year - 1983
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(83)80190-2
Subject(s) - calmodulin , atpase , chemistry , membrane , biochemistry , microsome , calcium , calcium atpase , biophysics , microbiology and biotechnology , botany , biology , enzyme , organic chemistry
The properties of the Ca‐ATPase prepared from roots of wheat seedlings treated with benzylaminopurine were studied. The affinity of the ATPase towards Ca 2+ , plant or erythrocyte calmodulin increased after the hormonal treatment. It seems that in the membrane calmodulin‐bonding sites were induced by benzylaminopurine, contributing to an increased affinity of the ATPase. The lower Ca‐content of the hormone‐treated plants suggests that in vivo the Ca‐ATPase is involved in a Ca‐extrusion process.