Abstract
EBASHI discovered that EGTA or Ca++ insensitive, non-relaxing actomyosin could be made EGTA sensitive by a third protein which exhibited physico-chemical properties characteristic of Bailey's tropomyosin B (ref. 1). However, he found no EGTA-sensitizing activity in Bailey's tropomyosin, and his new protein lost its activity when subjected to Bailey's procedures required for purification. Ebashi concluded that his EGTA-sensitizing protein was a new ‘tropomyosin-like’ protein or a native form of tropomyosin B. He offered no explanation concerning the difference between his ‘tropomyosin-like’ EGTA-sensitizing protein and Bailey's tropomyosin B.
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MUELLER, H. Effect of Bailey's Tropomyosin Purification on EGTA-sensitizing Activity. Nature 209, 1128–1129 (1966). https://doi.org/10.1038/2091128a0
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DOI: https://doi.org/10.1038/2091128a0
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