Nonparallel Isometric Tension Response of Rabbit Soleus Skinned Muscle Fibers to Magnesium Adenosine Triphosphate and Magnesium Inosine Triphosphate
ثبت نشده
چکیده
It has long been accepted that M g A T P is the energy source for contraction. Evidence has also accumulated indicating that M g A T P plays an important role in the regulation of contraction (Weber and Murray, 1973; Inoue and Tonomura , 1974; Godt, 1974; Orentlicher et al., 1977). In an a t tempt to better understand the dual role of ATP in contraction, several researchers have studied the effects on contraction of replacing ATP in contracting solutions with other nucleotides such as ITP, UTP , and G T P (Weber, 1969; Reuben et al., 1971). Two measures associated with muscle contraction have been used, hydrolysis of nucleotide by myosin and isometric tension development by skinned muscle fibers. An implied assumption in these nucleotide replacement studies is that the muscle will use and react to these nucleotides in an analogous fashion, and that differences in muscle response reflect quanti tat ive but not qualitative differences.-ia the rate processes governing muscle contraction. From the studies examining nucleotide hydrolysis by rabbit myofibrils and J. GEN. PHYSIOL. (~) The Rockefeller University Press 9 0022-1295/79/08/0261/14 $1.00 261 Volume 74 August 1979 261-274 on Jne 7, 2017 D ow nladed fom Published August 1, 1979
منابع مشابه
Nonparallel isometric tension response of rabbit soleus skinned muscle fibers to magnesium adenosine triphosphate and magnesium inosine triphosphate
The isometric tension response of single "skinned' rabbit soleus muscle fibers to MgATP and McITP in the absence of calcium was studied. [MgATP] or [MgITP] was varied in solutions of ionic strength 0.30 and temperature 20 degrees C. Steady-state tension that developed in MgATP or MgITP solutions was a biphasic bell-shaped function of log [MgATP] or log [MgITP] which increased from zero to maxim...
متن کاملThe effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers.
We have studied the effect of myosin P-light chain phosphorylation on the isometric tension generated by skinned fibers from rabbit psoas muscle at 0.6 and 10 microM Ca2+. At the lower Ca2+ concentration, which produced 10-20% of the maximal isometric tension obtained at 10 microM Ca2+, addition of purified myosin light chain resulted in a 50% increase in isometric tension which correlated with...
متن کاملCalcium-Activated Tension of Skinned Muscle Fibers of the Frog
The influence of MgATP on the Ga(++)-activated isometric tension of skinned frog muscle fibers was examined in solutions containing: Mg(++) = 5 mM, creatine phosphate (CP) = 14.5 mM, creatinephosphokinase (CPK) = 1 mg/ml, total EGTA = 7 mM, CaCl(2), KCl, imidazole >/= 20 mM so that ionic strength = 0.15, pH = 7.00, and MgATP = 2 mM, 0.1 mM, or 20 microM. CP and CPK were necessary for these expe...
متن کاملEffects of Magnesium and Calcium on the Superprecipitation of Myosin B.
The effects of magnesium and calcium on the adenosine triphosphate-induced contraction of glycerinated muscle fibers were recently reexamined. Magnesium and calcium were both shown to have a dual effect on the contractility of glycerinated fibers (1). By using myosin B suspensions in place of glycerinated fibers, we compared the dual effect of magnesium on the contractile phenomenon called “sup...
متن کاملCharacteristics of Ca2+- and Mg2+-induced tension development in chemically skinned smooth muscle fibers
Chemically skinned fibers from guinea pig taenia caecum were prepared by saponin treatment to study the smooth muscle contractile system in a state as close to the living state as posible. The skinned fibers showed tension development with an increase of Ca2+ in the solution, the threshold tension occurring as 5 X 10(-7) M Ca2+. The maximal tension induced with 10(-4) M Ca2+ was as large and ra...
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:
دوره شماره
صفحات -
تاریخ انتشار 2003