Comparative Studies of Light Meromyosin Paracrystals Derived from Red, White, and Cardiac Muscle Myosins
نویسندگان
چکیده
Tryptic and chymotryptic light meromyosin paracrystals from red and cardiac muscles of rabbit show a negative and positive staining pattern with uranyl acetate and phosphotungstate that sharply differs from that of white muscle light meromyosin paracrystals. The main periodicity of about 430 A is the same regardless of the source of light meromyosin. The results are discussed in terms of the molecular structure and the functional properties of various myosins.
منابع مشابه
Some Properties of Embryonic Myosin
Myosins from the following sources were purified by diethylaminoethyl-Sephadex chromatography: moytubes grown in vitro for 7-8 days, prepared from pectoralis muscles of 10-day old embryos, and breast and leg muscles from 16-day old embryos. The adenosine triphosphatase activities of these myosins were close to that of adult m. pectoralis myosin. The light chains of the embryonic myosins had the...
متن کاملInteraction between vertebrate skeletal and uterine muscle myosins and light meromyosins
The specific contributions of this work may be summarized as follows: (a) No hybridization of uterine and skeletal myosin occurs at pH 6.0 although previous studies have shown that hybridization does occur at pH 6.5 (B. Kaminer et al. 1976. J. Mol. Biol. 100:379-386) or 7.0 (T. Pollard. 1975. J. Cell Biol. 67:93-104) (b) Hybridization of uterine and skeletal light meromyosins (LMM) occurs at pH...
متن کاملThe axial repeats in paracrystals of light meromyosin and its complex with C-protein.
We examined the axial repeats in electron micrographs of three types of negatively stained paracrystals (two tactoid- and one sheet-like type) of rabbit light meromyosin (LMM) and its complex with C-protein characterized previously by similar axial period of about 43.0 nm. Assuming for the axial repeat in type II tactoids the value of 42.93 +/- 0.05 nm as it was determined by X-ray diffraction ...
متن کاملAdenosinetriphosphatase activity of cardiac myosin. Comparison of the enzymatic activities and activation by actin of dog cardiac, rabbit cardiac, rabbit white skeletal and rabbit red skeletal muscle myosins.
Examination of the ATPase activities of rabbit cardiac, rabbit red skeletal and rabbit white skeletal muscle myosins has demonstrated the existence of two types of myosin. One type, characterized by the higher ATPase activity, is present in white skeletal muscle; the other is found in red skeletal and cardiac muscle. The differences between myosin preparations could not be attributed to varying...
متن کاملLight meromyosin paracrystal formation
STUDIES OF PARACRYSTAL FORMATION BY COLUMN PURIFIED LIGHT MEROMYOSIN (LMM) PREPARED IN A VARIETY OF WAYS LED TO THE FOLLOWING CONCLUSIONS: (a) different portions of the myosin rod may be coded for different stagger relationships. This was concluded from observations that paracrystals with different axial repeat periodicities could be obtained either with LMM framents of different lengths prepar...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Journal of Cell Biology
دوره 49 شماره
صفحات -
تاریخ انتشار 1971