1984
DOI: 10.1021/bi00301a018
|View full text |Cite
|
Sign up to set email alerts
|

Binding of .beta.-scorpion toxin: a physicochemical study

Abstract: The binding to rat brain synaptosomes of a beta-scorpion toxin, i.e., toxin II of Centruroides suffusus suffusus (Css II), was studied as a function of pH, temperature, and concentration of some monovalent and divalent cations. At 10 degrees C and pH 6.0, the specific binding of 125I-labeled Css II corresponds to a single class of noninteracting high-affinity binding sites (KD = 0.18 nM) with a capacity (4.2 pmol/mg of protein) that is almost identical with that generally accepted for saxitoxin. The equilibriu… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
14
0

Year Published

1985
1985
2013
2013

Publication Types

Select...
10

Relationship

1
9

Authors

Journals

citations
Cited by 30 publications
(15 citation statements)
references
References 24 publications
1
14
0
Order By: Relevance
“…The apparent equilibrium dissociation constant (K d ϭ 0.73 Ϯ 0.11 nM; n ϭ 4) was independent of membrane potential and was not affected by pH changes between 6 and 8 (data not shown). These results are in concert with those published previously for native Css4 and Css2, in which the apparent affinity for rat brain synaptosomes was in the range between 0.56 and 0.79 nM (14,27). Cleavage of the N-terminal addition off Css4 by thrombin followed by HPLC purification yielded a recombinant Css4 product, rCss4, with only 4 additional residues at the N-terminal side.…”
Section: Expression and Characterization Of Recombinantsupporting
confidence: 90%
“…The apparent equilibrium dissociation constant (K d ϭ 0.73 Ϯ 0.11 nM; n ϭ 4) was independent of membrane potential and was not affected by pH changes between 6 and 8 (data not shown). These results are in concert with those published previously for native Css4 and Css2, in which the apparent affinity for rat brain synaptosomes was in the range between 0.56 and 0.79 nM (14,27). Cleavage of the N-terminal addition off Css4 by thrombin followed by HPLC purification yielded a recombinant Css4 product, rCss4, with only 4 additional residues at the N-terminal side.…”
Section: Expression and Characterization Of Recombinantsupporting
confidence: 90%
“…There is a drastic loss of pharmacological activity and binding to synaptosomes (<0.1% residual binding) when Lys-58 is biotinylated (or when the equivalent Lys-56 of AaH I is acetylated) (21,37). In addition to the chemical reactions affecting Lys-58, only modification of the basic residue in position 2, or removal of the N-terminal dipeptide, can result in comparably low residual activities (-1%).…”
Section: Resultsmentioning
confidence: 99%
“…It is well described in the literature that these peptides are modulators of Na + -channel activity [15], [16], [61]. These peptides are commonly found in scorpions of the family Buthidae [32], [34], [62], and are responsible for intoxication with serious medical problems, because they affect Na + -channels of excitable tissue causing membrane depolarization, liberation of neurotransmitters, which then affect the proper functioning of several organs that might lead to respiratory distress or heart failure, the two most common cause of dead [63], [64]. These peptides contain between 58 to 76 amino acid residues, tightly stabilized by four disulflide bridges [11].…”
Section: Discussionmentioning
confidence: 99%