Snake venom cardiotoxin induces G-actin polymerization

Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl 2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl 2 was present in the buffe...

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Bibliographic Details
Published inBiochimica et biophysica acta Vol. 966; no. 2; pp. 266 - 268
Main Authors Chen, Yee-Hsiung, Chu, Sin-Tak
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 11.08.1988
Elsevier
North-Holland
Subjects
Actin polymerization
Actins - metabolism
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Biopolymers - metabolism
Cardiotoxin
Cobra Cardiotoxin Proteins - pharmacology
Contractile proteins
Elapid Venoms - pharmacology
Fundamental and applied biological sciences. Psychology
Holoproteins
In Vitro Techniques
Muscles - drug effects
Muscles - metabolism
Proteins
Rabbit skeletal muscle
Rabbits
Snake venom
Cardiotoxin
Snake venom
Actin polymerization
Rabbit skeletal muscle
Vertebrata
Mammalia
Basic protein
Venom
Actins
Rabbit
Polymerization
Molecular interaction
Reptilia
Lagomorpha
Striated muscle
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Summary:Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl 2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl 2 was present in the buffer and could be inhibited if G-actin was preincubated with deoxyribonuclease I. Furthermore, the DNAase could also partially depolymerize actin polymer previously formed by the interaction of G-actin with the toxin.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/0304-4165(88)90120-1