Ryanodine receptor purified from crayfish skeletal muscle.
نویسندگان
چکیده
The ryanodine receptor was isolated from the sarcoplasmic reticulum of crayfish skeletal muscle. Ryanodine binding to the native fraction was measured by Scatchard analysis and values of 60 nmol/l and 9 pmol/mg were obtained for KD and Bmax respectively. The identity of purified receptor was confirmed by electron microscopy, electrophoresis and incorporation into planar lipid bilayers. At least two conductance states (100 pS and 50 pS) were observed in 100 mmol/l NaCl both for native and purified receptor.
منابع مشابه
Purified ryanodine receptor from skeletal muscle sarcoplasmic reticulum is the Ca2+-permeable pore of the calcium release channel.
The ryanodine receptor of rabbit skeletal muscle sarcoplasmic reticulum was purified by immunoaffinity chromatography as a single approximately 450,000-Da polypeptide and it was shown to mediate single channel activity identical to that of the ryanodine-treated Ca2+ release channel of the sarcoplasmic reticulum. The purified receptor had a [3H]ryanodine binding capacity (Bmax) of 280 pmol/mg an...
متن کاملCRAYFISH SKELETAL MUSCLE REQUIRES BOTH INFLUX OF EXTERNAL Ca2+ AND Ca2+ RELEASE FROM INTERNAL STORES FOR CONTRACTION
The isometric tension and membrane potential of single skeletal muscle fibres from the flexor muscle of the carpopodite in the meropodite of crayfish Procambarus clarkii (Girard) were studied to determine whether crayfish muscle contraction requires Ca2+ release from the sarcoplasmic reticulum. Contraction elicited by brief extracellular electrical stimulation was reduced by the removal of Ca2+...
متن کاملSuramin and suramin analogs activate skeletal muscle ryanodine receptor via a calmodulin binding site.
Contraction of skeletal muscle is triggered by the rapid release of Ca2+ from the sarcoplasmic reticulum via the ryanodine receptor/calcium-release channel. The trypanocidal drug suramin is an efficient activator of the ryanodine receptor. Here, we used high-affinity [3H]ryanodine binding to sarcoplasmic reticulum from rabbit skeletal muscle to screen for more potent analogs of suramin. This ap...
متن کاملActivation of the skeletal muscle ryanodine receptor by suramin and suramin analogs.
Ca2+ release from skeletal muscle sarcoplasmic reticulum is activated by adenine nucleotides and suramin. Because suramin is known to interact with ATP-binding enzymes and ATP receptors (P2-purinergic receptors), the stimulation by suramin has been postulated to occur via the adenine nucleotide-binding site of the ryanodine receptor/Ca2+-release channel. We tested this hypothesis using suramin ...
متن کاملA simple, fast, one-step method for the purification of the skeletal-muscle ryanodine receptor.
In this paper we describe a simple, fast, one-step method for the purification of the skeletal-muscle ryanodine receptor. The ryanodine receptor from CHAPS-solubilized junctional sarcoplasmic-reticulum membranes was adsorbed to a spermine-agarose column and eluted by 2 mM-spermine. The purified receptor, consisting predominantly of a 450 kDa polypeptide on SDS/PAGE, binds [3H]ryanodine with a s...
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:
- General physiology and biophysics
دوره 9 5 شماره
صفحات -
تاریخ انتشار 1990