EVIDENCE FOR CALCIUM‐SENSITIVE COMPONENT IN BRAIN ACTOMYOSIN‐LIKE PROTEIN (NEUROSTENIN)
- 1 September 1974
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 23 (3) , 497-501
- https://doi.org/10.1111/j.1471-4159.1974.tb06051.x
Abstract
Abstract— The isolation of brain actomyosin‐like protein (neurostenin) with a Ca2+ ‐sensitive component is described. The addition of 1 mm EGTA results in approximately 50 per cent reduction in MgATPase activity. The inhibition can be released by a free Ca2+ concentration of 10−6m. Dialysis of the protein complex against low ionic strength medium followed by centrifugation results in a loss of Ca2+ sensitivity in the pelleted protein. Ca2+ sensitivity can be restored by reprecipitating this desensitized complex in the presence of the 70.000 g supernatant. The protection of sulphhydryl groups during desensitization and reconstitution procedures is essential. This Ca2+ regulatory property is similar, in these respects, to other actomyosin‐like proteins.Keywords
This publication has 24 references indexed in Scilit:
- New Mode of AerodynamicsNature, 1973
- Actomyosin-Like Protein in BrainScience, 1973
- A contractile protein possessing Ca2+ sensitivity (natural actomyosin) from leucocytes. Its extraction and some of its propertiesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
- Uterine smooth muscle: TroponinArchives of Biochemistry and Biophysics, 1971
- Changes in the properties of myosin associated with muscle developmentBiochemistry, 1971
- Calcium binding by the troponin complex, and the purification and properties of troponin ABiochimica et Biophysica Acta (BBA) - Protein Structure, 1971
- Release of dopamine β-hydroxylase and chromogranin A upon stimulation of the splenic nerveTissue and Cell, 1970
- Modification of transmitter release by electrical interference with motor nerve endingsProceedings of the Royal Society of London. B. Biological Sciences, 1967
- The effect of calcium on acetylcholine release from motor nerve terminalsProceedings of the Royal Society of London. B. Biological Sciences, 1965