Heart contains two substrates (Mr = 40,000 and 41,000) for pertussis toxin-catalyzed ADP-ribosylation that co-purify with Ns

Craig C. Malbon; Thomas J. Mangano; David C. Watkins

doi:10.1016/0006-291X(85)90119-6

Heart contains two substrates (M_r = 40,000 and 41,000) for pertussis toxin-catalyzed ADP-ribosylation that co-purify with N_s

Craig C. Malbon
, Thomas J. Mangano
, David C. Watkins

Pharmacological Sciences

Stony Brook University

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

Two peptides (M_r = 40,000 and 41,000) in membranes of rabbit heart are radiolabeled when the membranes are incubated in the presence of activated pertussis toxin and [³²P]NAD⁺. The 41,000-M_r peptide appears to be the alpha subunit of the inhibitory regulatory protein of adenylate cyclase, N_i. The 40,000-M_r substrate for pertussis toxin in the heart was investigated. Purification of the stimulatory regulatory protein of adenylate cyclase, N_s, results in the co-purification of the alpha subunits of both N_s and N_i, the putative beta- (M_r = 35,000) and gamma- (M_r ≅ 15,000) subunits of N_s and N_i, and the additional 40,000-M_r peptide that is ADP-ribosylated by pertussis toxin. This 40,000-M_r substrate for pertussis toxin action appears to be a major N-protein of mammalian heart.

Original language	English
Pages (from-to)	809-815
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	128
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(85)90119-6
State	Published - Apr 30 1985

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title = "Heart contains two substrates (Mr = 40,000 and 41,000) for pertussis toxin-catalyzed ADP-ribosylation that co-purify with Ns",

abstract = "Two peptides (Mr = 40,000 and 41,000) in membranes of rabbit heart are radiolabeled when the membranes are incubated in the presence of activated pertussis toxin and [32P]NAD+. The 41,000-Mr peptide appears to be the alpha subunit of the inhibitory regulatory protein of adenylate cyclase, Ni. The 40,000-Mr substrate for pertussis toxin in the heart was investigated. Purification of the stimulatory regulatory protein of adenylate cyclase, Ns, results in the co-purification of the alpha subunits of both Ns and Ni, the putative beta- (Mr = 35,000) and gamma- (Mr ≅ 15,000) subunits of Ns and Ni, and the additional 40,000-Mr peptide that is ADP-ribosylated by pertussis toxin. This 40,000-Mr substrate for pertussis toxin action appears to be a major N-protein of mammalian heart.",

author = "Malbon, \{Craig C.\} and Mangano, \{Thomas J.\} and Watkins, \{David C.\}",

year = "1985",

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doi = "10.1016/0006-291X(85)90119-6",

language = "English",

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TY - JOUR

T1 - Heart contains two substrates (Mr = 40,000 and 41,000) for pertussis toxin-catalyzed ADP-ribosylation that co-purify with Ns

AU - Malbon, Craig C.

AU - Mangano, Thomas J.

AU - Watkins, David C.

PY - 1985/4/30

Y1 - 1985/4/30

N2 - Two peptides (Mr = 40,000 and 41,000) in membranes of rabbit heart are radiolabeled when the membranes are incubated in the presence of activated pertussis toxin and [32P]NAD+. The 41,000-Mr peptide appears to be the alpha subunit of the inhibitory regulatory protein of adenylate cyclase, Ni. The 40,000-Mr substrate for pertussis toxin in the heart was investigated. Purification of the stimulatory regulatory protein of adenylate cyclase, Ns, results in the co-purification of the alpha subunits of both Ns and Ni, the putative beta- (Mr = 35,000) and gamma- (Mr ≅ 15,000) subunits of Ns and Ni, and the additional 40,000-Mr peptide that is ADP-ribosylated by pertussis toxin. This 40,000-Mr substrate for pertussis toxin action appears to be a major N-protein of mammalian heart.

AB - Two peptides (Mr = 40,000 and 41,000) in membranes of rabbit heart are radiolabeled when the membranes are incubated in the presence of activated pertussis toxin and [32P]NAD+. The 41,000-Mr peptide appears to be the alpha subunit of the inhibitory regulatory protein of adenylate cyclase, Ni. The 40,000-Mr substrate for pertussis toxin in the heart was investigated. Purification of the stimulatory regulatory protein of adenylate cyclase, Ns, results in the co-purification of the alpha subunits of both Ns and Ni, the putative beta- (Mr = 35,000) and gamma- (Mr ≅ 15,000) subunits of Ns and Ni, and the additional 40,000-Mr peptide that is ADP-ribosylated by pertussis toxin. This 40,000-Mr substrate for pertussis toxin action appears to be a major N-protein of mammalian heart.

UR - https://www.scopus.com/pages/publications/0022434612

U2 - 10.1016/0006-291X(85)90119-6

DO - 10.1016/0006-291X(85)90119-6

M3 - Article

C2 - 3922367

AN - SCOPUS:0022434612

SN - 0006-291X

VL - 128

SP - 809

EP - 815

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Heart contains two substrates (M_r = 40,000 and 41,000) for pertussis toxin-catalyzed ADP-ribosylation that co-purify with N_s

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