Paramyosin fibrils from the adductor muscles of Venus mercenaria are soluble above neutrality at relatively high ionic strength. From this viscous solution it is possible, by reduction in ionic strength, to reprecipitate acicular crystals of paramyosin. In the electron microscope these fibrils manifest a symmetrical band pattern similar to that previously described by Hodge but differing in some details. The axial periods observed under the conditions of the experiment varied between 1700 and 2000 A and a simple band pattern of one-fifth the main period was frequently observed. ATPase activity of the myosin type but of much lower intensity was demonstrated. Tryptic fission of the protein occurs but the characteristics differ from those of myosin.
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25 November 1957
Content prior to 1962 was published under the journal name
The Journal of Biophysical and Biochemical Cytology
Article|
November 25 1957
SOME CHEMICAL AND STRUCTURAL PROPERTIES OF PARAMYOSIN
Ronald H. Locker,
Ronald H. Locker
From the Biology Department, Massachusetts Institute of Technology, Cambridge
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Francis O. Schmitt
Francis O. Schmitt
From the Biology Department, Massachusetts Institute of Technology, Cambridge
Search for other works by this author on:
Ronald H. Locker
From the Biology Department, Massachusetts Institute of Technology, Cambridge
Francis O. Schmitt
From the Biology Department, Massachusetts Institute of Technology, Cambridge
Received:
June 26 1957
Copyright, 1957, by The Rockefeller Institute for Medical Research
1957
J Biophys and Biochem Cytol (1957) 3 (6): 889–896.
Article history
Received:
June 26 1957
Citation
Ronald H. Locker, Francis O. Schmitt; SOME CHEMICAL AND STRUCTURAL PROPERTIES OF PARAMYOSIN . J Biophys and Biochem Cytol 25 November 1957; 3 (6): 889–896. doi: https://doi.org/10.1083/jcb.3.6.889
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