High and low affinity Ca2+ binding to the sarcoplasmic reticulum: use of a high-affinity fluorescent calcium indicator
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چکیده
منابع مشابه
Activation and inhibition of the calcium gate of sarcoplasmic reticulum by high-affinity ryanodine binding.
The occupancy of high-affinity ryanodine-binding sites of isolated heavy sarcoplasmic reticulum vesicles occurring in concentrated salt solutions affects ATP-dependent calcium accumulation and caffeine-induced calcium release. The initial suppression of calcium uptake is followed by a marked uptake activation resulting in a reduction of the final calcium level in the medium. Simultaneously, caf...
متن کاملIsolation of a high affinity calcium-binding protein from sarcoplasmic reticulum.
Seven proteins have been isolated from sarcoplasmic reticulum. These proteins have been identified as an ATPase, a series of water soluble, acidic proteins of molecular weights 55,000, 46,500, 38,000, 33,000, and 20,000, and a proteolipid. The interactions of the acidic proteins with Ca2+ have been measured at pH 7.5 in the presence and absence of 0.1 M KCl. The protein of molecular weight 55,0...
متن کاملLow affinity calcium binding sites of the calcium transport ATPase of sarcoplasmic reticulum membranes.
Calcium binding sites having low affinity constants of less than 10(3) M-1 were titrated in native sarcomplasmic reticulum vesicles as well as in lipid deprived membranes and in the isolated calcium transport ATPase. Short time calcium binding measurements and the determination of the calcium binding heat allow to distinguish low affinity calcium binding sites located on the external surface of...
متن کاملTrypsin destruction of the high affinity ryanodine binding sites of the junctional sarcoplasmic reticulum.
Tryptic digestion of the junctional sarcoplasmic reticulum membranes in sucrose but not NaCl buffer leads to complete loss of ryanodine binding capacity. The presence of MgCl2 in the sucrose buffer prevents the loss of ryanodine binding by the trypsin treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the treated membranes reveal that the 400-kDa protein band disappeared un...
متن کاملIdentification and characterization of the high affinity [3H]ryanodine receptor of the junctional sarcoplasmic reticulum Ca2+ release channel.
The high affinity ryanodine receptor of the Ca2+ release channel from junctional sarcoplasmic reticulum of rabbit skeletal muscle has been identified and characterized using monoclonal antibodies. Anti-ryanodine receptor monoclonal antibody XA7 specifically immunoprecipitated [3H]ryanodine-labeled receptor from digitonin-solubilized triads in a dose-dependent manner. [3H]Ryanodine binding to th...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1977
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(77)85592-6