Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Batrachotoxinin-A 20-α-benzoate: A new radioactive ligand for voltage sensitive sodium channels (1981)
    Springer
    Cellular and molecular neurobiology 1 (1981), S. 19-40 
    Details
    ISSN: 1573-6830
    Keywords: batrachotoxin ; batrachotoxinin-A 20-α-benzoate ; sodium channels ; depolarizing agents ; tetrodotoxin ; scorpion toxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Batrachotoxinin-A 20-α-benzoate (BTX-B), an analog of the potent depolarizing agent batrachotoxin (BTX), was prepared by selective esterification of naturally occurring batrachotoxinin-A with benzoic acid. BTX-B depolarizes rat phrenic nerve-diaphragm preparations with a time course and concentration dependence virtually indistinguishable from that of BTX. A specific, saturable component of equilibrium binding of [3H]BTX-B to mouse cerebral cortex homogenates was measured, described by an equilibrium dissociation constant of 0.7 µM and a maximum number of binding sites of 90 pmol per gram of tissue (wet weight). Specific binding is inhibited by BTX and other BTX analogs, veratridine, and grayanotoxin but is unaffected by tetrodotoxin and cevine. Under conditions of this assay, neither crude Leiurus quinquestriatus scorpion venom nor purified sea anemone toxin have any effect on specific binding. The data support the conclusion that BTX-B interacts with a recognition site associated with voltage sensitive sodium channels which is identical to the recognition site for BTX.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00736037
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Interaction of batrachotoxinin-A benzoate with voltage-sensitive sodium channels: The effects of pH (1981)
    Springer
    Cellular and molecular neurobiology 1 (1981), S. 361-371 
    Details
    ISSN: 1573-6830
    Keywords: batrachotoxin ; batrachotoxinin-A-20-α-benzoate ; sodium channels ; pH ; histidine modification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The binding of labeled batrachotoxinin-A benzoate (BTX-B) to voltage-sensitive sodium channels in broken membrane preparations of mouse cerebral cortex has been measured as a function of the pH. Specific binding is negligible at pH 〈6.0, maximum at pH 8.5, and decreases again at pH 9.0. A major component of nonspecific binding, however, increases linearly in the pH range 7.0-9.0. The pK a of batrachotoxinin-A, an analogue of BTX-B, was found by titrimetric methods to be ≥8.2. Analysis of the data shows that at least part of the pH dependence of BTX-B binding is due to the titration of a sodium channel residue(s) associated in some way with the BTX-B recognition site. The possible involvement of a histidine residue is suggested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00716271
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Effect of histrionicotoxin on ion channels in synaptic and conducting membranes of electroplax ofElectrophorus electricus (1983)
    Springer
    Cellular and molecular neurobiology 3 (1983), S. 203-212 
    Details
    ISSN: 1573-6830
    Keywords: batrachotoxin ; histrionicotoxin ; acetylcholine ; sodium channels ; local anesthetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Histrionicotoxin (HTX) at low concentrations of 5–10µM blocks the postsynaptic potential of the electroplax ofElectrophorus electricus. 2. At 100-fold higher concentrations, HTX blocks the directly evoked action potentials of the conducting membrane. 3. The pH dependence of the blockade by HTX at synaptic channels is different from that at the conducting membrane. At the synapse HTX is more potent at acid pH, while at the conducting membrane it is more potent at basic pH. 4. HTX at high concentrations antagonizes the effects of batrachotoxin, indicative of an effect on the batrachotoxin-sensitive sodium channels involved in action potential generation. 5. While the effects of HTX on the synaptic channels are concentration, time, and pH dependent, the effects on the channels of the conducting membrane are, in addition, use dependent, suggesting interactions of HTX with the activated forms of these channels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00710947
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...