Characterization of High Affinity Binding Sites for Charybdotoxin in Sarcolemmal Membranes from Bovine Aortic Smooth Muscle

This publication has 32 references indexed in Scilit:

• High levels of sodium-calcium exchange in vascular smooth muscle sarcolemmal membrane vesicles
  Biochemistry, 1989
• Potassium blocks barium permeation through a calcium-activated potassium channel.
  The Journal of general physiology, 1988
• Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel.
  The Journal of general physiology, 1988
• Charybdotoxin block of single Ca2+-activated K+ channels. Effects of channel gating, voltage, and ionic strength.
  The Journal of general physiology, 1988
• Trapping single ions inside single ion channels
  Biophysical Journal, 1987
• Identification of two toxins from scorpion (Leiurus quinquestriatus) venom which block distinct classes of calcium‐activated potassium channel
  FEBS Letters, 1986
• Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle
  Nature, 1985
• Molecular properties of the apamin‐binding component of the Ca²⁺‐dependent K⁺ channel Radiation‐inactivation, affinity labelling and solubilization
  European Journal of Biochemistry, 1984
• Quantitative analysis of drug-receptor interactions: I. Determination of kinetic and equilibrium properties
  Life Sciences, 1981
• Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
  Biochemical Pharmacology, 1973