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Inhibition of chloroplast adenosine triphosphatase activity by basic proteins and peptides
Author(s) -
Hasebe Hiroshi,
Yamazaki Shojiro,
Tamaura Yutaka,
Hagiwara Hiromi,
Inada Yuji
Publication year - 1978
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(78)81014-x
Subject(s) - chemistry , chemical technology , library science , polymer science , engineering , computer science , biochemical engineering
and myofibrils [4] have been extensively studied to clarify the mech- anism of energy transducing systems. In our laboratory, we demonstrated that troponin component TN-I, ‘which is an inhibitor of actomyosin ATPase, strongly inhibits the mitochondrial and chloroplast ATPase activities [S-7]. Mitochondrial ATPase inhibitor (Fr- inhibitor) also inhibited the chloroplast and acto- myosin ATPase activities [8,9] as well as the mito- chondrial ATPase activity. These results showed the similarity of the action of ATPase inhibitors on ATPases obtained from different sources with a system of heterogeneous combination. The actomyosin ATPase activity was reported [lo] to be inhibited by basic proteins such as salmine, lysozyme and cytochrome c. It is demon- strated here that the chloroplast ATPase activity is inhibited by basic proteins and peptides and that the inhibitory action is due to ammo groups in the molecule of inhibitor proteins.