Identification of Myosin in Nitella flexilis
A myosin B-like protein was extracted from the alga Nitella flexilis . SDS-polyacrylamide gel electrophoresis revealed the presence of myosin heavy chain and actin as the main components. At high ionic strength, its ATPase [EC 3.6.1.3] reaction was activated by EDTA or Ca2+ and inhibited by Mg2+ At...
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fthighwire:oai:open-archive.highwire.org:jbiochem:82/3/777 2023-05-15T17:23:48+02:00 Identification of Myosin in Nitella flexilis KATO, Toyoki TONOMURA, Yuji 1977-09-01 00:00:00.0 text/html http://jb.oxfordjournals.org/cgi/content/short/82/3/777 en eng Oxford University Press http://jb.oxfordjournals.org/cgi/content/short/82/3/777 Copyright (C) 1977, Japanese Biochemical Society Articles TEXT 1977 fthighwire 2016-11-16T17:46:45Z A myosin B-like protein was extracted from the alga Nitella flexilis . SDS-polyacrylamide gel electrophoresis revealed the presence of myosin heavy chain and actin as the main components. At high ionic strength, its ATPase [EC 3.6.1.3] reaction was activated by EDTA or Ca2+ and inhibited by Mg2+ At low ionic strength, superprecipitation was induced by the addition of ATP. Myosin was purified from Nitella myosin B. The molecular weight of the heavy chain of Nitella myosin, estimated by SDS-gel electrophoresis, was slightly higher than that of skeletal muscle myosin. At low ionic strength, Nitella myosin aggregated to form bipolar filaments about 0.2 μm long. At high ionic strength, its ATPase reaction was activated by EDTA or Ca2+ and inhibited by Mg2+ The Mg2+ reaction of Nitella myosin was activated by skeletal muscle F-actin. Text Nitella flexilis HighWire Press (Stanford University) |
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Articles KATO, Toyoki TONOMURA, Yuji Identification of Myosin in Nitella flexilis |
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A myosin B-like protein was extracted from the alga Nitella flexilis . SDS-polyacrylamide gel electrophoresis revealed the presence of myosin heavy chain and actin as the main components. At high ionic strength, its ATPase [EC 3.6.1.3] reaction was activated by EDTA or Ca2+ and inhibited by Mg2+ At low ionic strength, superprecipitation was induced by the addition of ATP. Myosin was purified from Nitella myosin B. The molecular weight of the heavy chain of Nitella myosin, estimated by SDS-gel electrophoresis, was slightly higher than that of skeletal muscle myosin. At low ionic strength, Nitella myosin aggregated to form bipolar filaments about 0.2 μm long. At high ionic strength, its ATPase reaction was activated by EDTA or Ca2+ and inhibited by Mg2+ The Mg2+ reaction of Nitella myosin was activated by skeletal muscle F-actin. |
format |
Text |
author |
KATO, Toyoki TONOMURA, Yuji |
author_facet |
KATO, Toyoki TONOMURA, Yuji |
author_sort |
KATO, Toyoki |
title |
Identification of Myosin in Nitella flexilis |
title_short |
Identification of Myosin in Nitella flexilis |
title_full |
Identification of Myosin in Nitella flexilis |
title_fullStr |
Identification of Myosin in Nitella flexilis |
title_full_unstemmed |
Identification of Myosin in Nitella flexilis |
title_sort |
identification of myosin in nitella flexilis |
publisher |
Oxford University Press |
publishDate |
1977 |
url |
http://jb.oxfordjournals.org/cgi/content/short/82/3/777 |
genre |
Nitella flexilis |
genre_facet |
Nitella flexilis |
op_relation |
http://jb.oxfordjournals.org/cgi/content/short/82/3/777 |
op_rights |
Copyright (C) 1977, Japanese Biochemical Society |
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1766114267271004160 |