[Purification and biochemical characteristics of myosin from rat malignant sarcoma-45].
Myosin was purified from rat tumour sarcoma-45 whose properties (effects of cations on ATPase activity, substrate specificity, temperature- and pH-optima, thermal stability, sensitivity of Mg2(+)-ATPase to F-actin, molecular mass, subunit composition) are similar to those of fast skeletal muscle myosin. Some parameters of the protein, namely, the levels of Ca2(+)- and K+, EDTA-ATPase activity, relative content of myosin light chains with Mr 16500 and the degree of tumoural myosin Mg2(+)-ATPase activation by F-actin, were significantly lower than those of skeletal muscle myosin.
Senchuk
V V
VV
Pikulev
A T
AT
Sholukh
M V
MV
D000199:Actins / Q000032:analysis; D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009218:Myosins / Q000032:analysis / Q000302:isolation & purification*; D051381:Rats; D012513:Sarcoma, Experimental / Q000032:analysis* / Q000201:enzymology; D013379:Substrate Specificity
D000199:Actins; D000251:Adenosine Triphosphatases; D009218:Myosins
Ochistka i biokhimicheskaia kharakteristika miozina iz zlokachestvennoĭ opukholi krys sarkoma-45.