1956
DOI: 10.1042/bj0630337
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Some properties of the actomyosin-like protein of the uterus

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Cited by 63 publications
(11 citation statements)
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“…Preparation of the purified actomyosin. The early stages were similar to those described by Needham & Cawkwell (1956), except that when small quantities of tissue were used (20-30 g.) it was disintegrated at 40 by thorough grinding with acid-washed sand or quartz, the extracting fluid being added gradually. This had the advantage over the use of the Waring Blendor that frothing was avoided.…”
Section: Materia8mentioning
confidence: 76%
See 1 more Smart Citation
“…Preparation of the purified actomyosin. The early stages were similar to those described by Needham & Cawkwell (1956), except that when small quantities of tissue were used (20-30 g.) it was disintegrated at 40 by thorough grinding with acid-washed sand or quartz, the extracting fluid being added gradually. This had the advantage over the use of the Waring Blendor that frothing was avoided.…”
Section: Materia8mentioning
confidence: 76%
“…Cell-particle suspension. This was made as described by Needham & Cawkwell (1956). The residues obtained after centrifuging the 0-5M-KCI extract at 100 000 g always 1.…”
Section: Materia8mentioning
confidence: 99%
“…However, when added together the combination thus formed was sensitive, indicating that a thrombosthenin complex, analogous to muscle actomyosin, had formed. However, the ATPase activity of the thrombosthenin complex has been found to be 50 to 100 times below the values for muscle actomyosin (Hasselbach 1951) and 5-10 times lower than the values for the contractile protein of smooth muscle reported by Needham & Cawkwell (1956). Thrombosthenin differs also from muscle actomyosin in its immunological properties.…”
Section: Behnkementioning
confidence: 66%
“…Kielley & Meyerhof (1950) found the magnesium activated ATP-ase of muscle was inactivated by a phospholipase C preparation from Clostridium welchii, the splitting of phospholipid being proportional to the inactivation. On the other hand, the myosin ATP-ase appears to be unaffected (Macfarlane, 1950) and similarly a particulate ATP-ase prepared from rat uterus was found to be resistant to phospholipase attack (Needham & Cawkwell, 1956). Swanson & Mitchell (1952) have isolated a highly purified preparation of ATP-ase from liver nuclei which was especially rich in phospholipids (reported by Artom, Lehninger (1956) have found approximately 20% of phospholipid in a particulate fraction isolated from mitochondria which was able to carry out oxidative phosphorylation during the oxidation of /?-hydroxybutyric acid.…”
Section: (2) Structural Roles Especially In Cell Oxidasesmentioning
confidence: 99%