The 65-kDa protein from pig heart. A new substrate for Clostridium botulinum ADP-ribosyltransferase (exoenzyme C3)

S I Hoffenberg; V O Rybin; A N Efimenko; I N Kurochkin; V A Tkachuk

doi:10.1016/0014-5793(91)81152-x

The 65-kDa protein from pig heart. A new substrate for Clostridium botulinum ADP-ribosyltransferase (exoenzyme C3)

FEBS Lett. 1991 Nov 18;293(1-2):59-61. doi: 10.1016/0014-5793(91)81152-x.

Authors

S I Hoffenberg¹, V O Rybin, A N Efimenko, I N Kurochkin, V A Tkachuk

Affiliation

¹ USSR Research Center for Molecular Diagnostics and Therapy, Moscow.

PMID: 1959672
DOI: 10.1016/0014-5793(91)81152-x

Abstract

In the pig heart sarcolemma, a 65 kDa protein is found to be ADP-ribosylated by Clostridium botulinum ADP-ribosyltransferase (exoenzyme C3). ADP-ribosylation of this protein is regulated by guanyl nucleotides and cytosol factor in a fashion similar to that for other C3 substrates. The new exoenzyme C3 substrate was partially purified. This protein is supposed to be a GTP-binding one.

MeSH terms

ADP Ribose Transferases / isolation & purification
ADP Ribose Transferases / metabolism*
Animals
Bacterial Proteins / chemistry*
Bacterial Proteins / isolation & purification
Botulinum Toxins*
Clostridium botulinum / chemistry
Clostridium botulinum / enzymology*
GTP-Binding Proteins / analysis
Heart Ventricles / chemistry*
Hydrolysis
Molecular Weight
Sarcolemma / chemistry*
Substrate Specificity
Swine

Substances

Bacterial Proteins
ADP Ribose Transferases
exoenzyme C3, Clostridium botulinum
Botulinum Toxins
GTP-Binding Proteins