ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions.

T Meyer; R Koch; Werner Fanick; H Hilz

ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions.

Standard

ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions. / Meyer, T; Koch, R; Fanick, Werner; Hilz, H.

in: Biol Chem Hoppe Seyler, Jahrgang 369, Nr. 7, 7, 1988, S. 579-583.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Meyer, T, Koch, R, Fanick, W & Hilz, H 1988, 'ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions.', Biol Chem Hoppe Seyler, Jg. 369, Nr. 7, 7, S. 579-583. <http://www.ncbi.nlm.nih.gov/pubmed/3223989?dopt=Citation>

APA

Meyer, T., Koch, R., Fanick, W., & Hilz, H. (1988). ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions. Biol Chem Hoppe Seyler, 369(7), 579-583. [7]. http://www.ncbi.nlm.nih.gov/pubmed/3223989?dopt=Citation

Vancouver

Meyer T, Koch R, Fanick W, Hilz H. ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions. Biol Chem Hoppe Seyler. 1988;369(7):579-583. 7.

Bibtex

@article{ba2a474fde8d43e4a6c6034909352833,

title = "ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions.",

abstract = "Various types of ADP-ribosyl protein conjugates were synthesized and their chemical stability was compared with that of cysteine-linked ADP-ribosyl groups as formed by incubation of transducin or Gi/Go proteins with NAD and pertussis toxin. Treatment with 0.1 mM HgCl2 specifically cleaved the cysteine-linked conjugates. This may provide a tool for the quantitation of modified Gi/Go proteins as well as of other acceptors modified by ADP-ribose at cysteine residues in the presence of other ADP-ribosyl proteins.",

keywords = "Animals, Cattle, Hydrolysis, Adenosine Diphosphate Ribose/*metabolism, NAD/metabolism, Cysteine, Histones/*metabolism, Mercury/*pharmacology, Mitochondria, Heart/metabolism, Peptide Elongation Factor 2, Peptide Elongation Factors/metabolism, Peptides/*metabolism, *Pertussis Toxin, Proteins/*metabolism, Submitochondrial Particles/metabolism, Transducin/metabolism, Virulence Factors, Bordetella/*metabolism, Animals, Cattle, Hydrolysis, Adenosine Diphosphate Ribose/*metabolism, NAD/metabolism, Cysteine, Histones/*metabolism, Mercury/*pharmacology, Mitochondria, Heart/metabolism, Peptide Elongation Factor 2, Peptide Elongation Factors/metabolism, Peptides/*metabolism, *Pertussis Toxin, Proteins/*metabolism, Submitochondrial Particles/metabolism, Transducin/metabolism, Virulence Factors, Bordetella/*metabolism",

author = "T Meyer and R Koch and Werner Fanick and H Hilz",

year = "1988",

language = "English",

volume = "369",

pages = "579--583",

number = "7",

}

RIS

TY - JOUR

T1 - ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions.

AU - Meyer, T

AU - Koch, R

AU - Fanick, Werner

AU - Hilz, H

PY - 1988

Y1 - 1988

N2 - Various types of ADP-ribosyl protein conjugates were synthesized and their chemical stability was compared with that of cysteine-linked ADP-ribosyl groups as formed by incubation of transducin or Gi/Go proteins with NAD and pertussis toxin. Treatment with 0.1 mM HgCl2 specifically cleaved the cysteine-linked conjugates. This may provide a tool for the quantitation of modified Gi/Go proteins as well as of other acceptors modified by ADP-ribose at cysteine residues in the presence of other ADP-ribosyl proteins.

AB - Various types of ADP-ribosyl protein conjugates were synthesized and their chemical stability was compared with that of cysteine-linked ADP-ribosyl groups as formed by incubation of transducin or Gi/Go proteins with NAD and pertussis toxin. Treatment with 0.1 mM HgCl2 specifically cleaved the cysteine-linked conjugates. This may provide a tool for the quantitation of modified Gi/Go proteins as well as of other acceptors modified by ADP-ribose at cysteine residues in the presence of other ADP-ribosyl proteins.

KW - Animals

KW - Cattle

KW - Hydrolysis

KW - Adenosine Diphosphate Ribose/metabolism

KW - NAD/metabolism

KW - Cysteine

KW - Histones/metabolism

KW - Mercury/pharmacology

KW - Mitochondria, Heart/metabolism

KW - Peptide Elongation Factor 2

KW - Peptide Elongation Factors/metabolism

KW - Peptides/metabolism

KW - Pertussis Toxin

KW - Proteins/metabolism

KW - Submitochondrial Particles/metabolism

KW - Transducin/metabolism

KW - Virulence Factors, Bordetella/metabolism