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An ADP-ribosyltransferase from turkey erythrocytes which utilizes proteins and low molecular weight guanidino compounds such as arginine and agmatine as ADP-ribose acceptors was stimulated by histones. The effect was specific in that choleragen, a bacterial mono(ADP-ribosyl)transferase that increased adenylate cyclase activity in animal cells, was not activated by histones. With the erythrocyte enzyme, histones decreased the apparent Km values for arginine methyl ester and agmatine and increased the stability of the transferase to thermal denaturation. Activation of the transferase by histones was rapid, with a minimal delay observed upon addition of histones to a histone-free assay. Activation by histones was reversed upon dilution of a sample containing histones into an assay mix free of histone. In the absence of histone, the transferase existed as a rapidly sedimenting species; in the presence of histone, the transferase sedimented as a protomer.
J Moss, and
S J Stanley, and
J C Osborne
February 1997,
The Journal of biological chemistry,
J Moss, and
S J Stanley, and
J C Osborne
December 1992,
Proceedings of the National Academy of Sciences of the United States of America,
J Moss, and
S J Stanley, and
J C Osborne
September 1996,
The Journal of biological chemistry,
J Moss, and
S J Stanley, and
J C Osborne
April 1997,
The Journal of biological chemistry,
J Moss, and
S J Stanley, and
J C Osborne
March 1999,
Molecular and cellular biochemistry,
J Moss, and
S J Stanley, and
J C Osborne
May 1989,
The Journal of biological chemistry,
J Moss, and
S J Stanley, and
J C Osborne
November 2007,
Eukaryotic cell,
J Moss, and
S J Stanley, and
J C Osborne
April 1984,
The Biochemical journal,
J Moss, and
S J Stanley, and
J C Osborne
February 1986,
Analytical biochemistry,
J Moss, and
S J Stanley, and
J C Osborne
August 1991,
Biochemical and biophysical research communications,
