منابع مشابه
Relaxing messages from the sarcolemma
593 C o m m e n t a r y In spite of the detailed understanding reached in the last 50 years about the molecular mechanisms of muscle excitability, the localization of the Cl conductance, G Cl , in muscle has remained highly contended. In this issue, Lueck et al. address this long-standing controversy, measuring directly the Cl current mediated by the ClC-1 channel using the patch clamp tech...
متن کاملTHE Ca2+-ATPase OF HEART SARCOLEMMA
THE Ca2+-ATPase OF HEART SARCOLEMMA P. Caroni and E. Carafoli, Laboratory of Biochemistry, Swiss Federal Institute of Technology (ETH), Universitiitstr. 16, 8092 Zurich, Switzerland The Ca2+-ATPase of heart sarcolema (SL) has high affinity for Ca2+ (K,,, = 0.3uM), is slightly stimulated by K ' , has a (ATP) of 30uM, a pH optimum of 7.3 and is highly sensitive to vanadate (Ki= 0.6uM). The high v...
متن کاملAdenosine triphosphatase activities of muscle sarcolemma.
Isolated sarcolemma hydrolyzed ATP in the presence of Mg2+ and Ca2+. MgATPase was stimulated by low concentrations of Ca2+ and inhibited by high concentrations of this cation. Membranes hydrolyzed p-nitrophenylphosphate in the presence of Mg 2+; this activity was stimulated by Ca2f and K+. La3f stimulated MgATPase at low concentrations (up to 50 pM) and caused inhibition at higher concentration...
متن کاملIntact Vesicles of Canine Cardiac Sarcolemma
Most biological membranes are functionally asymmetric. To study biochemical control of cardiac transsarcolemmal ion fluxes, it would be of obvious advantage to use isolated vesicles of sarcolemma which retains the low passive permeability characteristics of intact sarcolemma because in such vesicles the membrane should exhibit its normal asymmetric character with respect to enzymic activities. ...
متن کاملCalcium binding by skeletal muscle sarcolemma.
Plasma membranes isolated from rabbit muscle possessed the ability to bind and accumulate calcium ions; these processes required ATP and Mg*+. Binding of Ca2+ was rapid, reaching a maximum within 30 s and was greatly increased in the presence of oxalate or phosphate. The concentrations of Ca2+, Mg2+, and ATP required for half-maximal ATP-dependent calcium binding were 20 KM, 150 PM, and 20 to 3...
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ژورنال
عنوان ژورنال: Science
سال: 1965
ISSN: 0036-8075,1095-9203
DOI: 10.1126/science.150.3705.1846-a