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פותח על ידי קלירמאש פתרונות בע"מ -
Immunochemical evidence for a novel pertussis toxin substrate in human neutrophils
Year:
1986
Source of publication :
Journal of Biological Chemistry
Authors :
פינס, מרק
;
.
Volume :
261
Co-Authors:
Gierschik, P., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States
Falloon, J., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States
Milligan, C., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States
Pines, M.
Gallin, J.I.
Spiegel, A.
Facilitators :
From page:
8058
To page:
8062
(
Total pages:
5
)
Abstract:
Pertussis toxin catalyzes incorporation of 20.2 pmol of ADP-ribose/mg of protein into approximately 40-kDa protein(s) in human neutrophil membranes compared with 14.1 pmol/mg in bovine brain membranes. Based on these measurements we estimate that pertussis toxin substrate(s) should represent at least 0.085% of total membrane protein in neutrophils. Both brain and neutrophil membranes show high concentrations (0.34 versus 0.16% of total membrane protein, respectively) of the common β subunit of guanine nucleotide binding proteins. Affinity purified antibodies specific for G(o)-α fail to detect any protein in immunoblots of neutrophil membranes (150 μg) under conditions where as little as 10 ng of purified G(o)-α is detectable, and G(o)-α is readily detected in brain membranes (100 μg). An antiserum against transducin that cross-reacts strongly with G(i)-α, detects as little as 5 ng of purified G(i)-α and readily detects G(i)-α in brain membranes, but in neutrophil membranes, the antiserum detects an approximately 40-kDa band that corresponds to less than 10% of the expected amount of pertussis toxin substrate(s). The results show that human neutrophil membranes contain relatively large amounts of pertussis toxin substrate(s), but that the predominant pertussis toxin substrate is immunochemically distinct from previously identified substrates, transducin, G(i), and G(o).
Note:
Related Files :
Animals
cattle
cell membrane
Cerebral Cortex
Neutrophils
Pertussis toxin
Phosphorus Radioisotopes
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
21392
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:43
You may also be interested in
Scientific Publication
Immunochemical evidence for a novel pertussis toxin substrate in human neutrophils
261
Gierschik, P., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States
Falloon, J., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States
Milligan, C., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States
Pines, M.
Gallin, J.I.
Spiegel, A.
Immunochemical evidence for a novel pertussis toxin substrate in human neutrophils
Pertussis toxin catalyzes incorporation of 20.2 pmol of ADP-ribose/mg of protein into approximately 40-kDa protein(s) in human neutrophil membranes compared with 14.1 pmol/mg in bovine brain membranes. Based on these measurements we estimate that pertussis toxin substrate(s) should represent at least 0.085% of total membrane protein in neutrophils. Both brain and neutrophil membranes show high concentrations (0.34 versus 0.16% of total membrane protein, respectively) of the common β subunit of guanine nucleotide binding proteins. Affinity purified antibodies specific for G(o)-α fail to detect any protein in immunoblots of neutrophil membranes (150 μg) under conditions where as little as 10 ng of purified G(o)-α is detectable, and G(o)-α is readily detected in brain membranes (100 μg). An antiserum against transducin that cross-reacts strongly with G(i)-α, detects as little as 5 ng of purified G(i)-α and readily detects G(i)-α in brain membranes, but in neutrophil membranes, the antiserum detects an approximately 40-kDa band that corresponds to less than 10% of the expected amount of pertussis toxin substrate(s). The results show that human neutrophil membranes contain relatively large amounts of pertussis toxin substrate(s), but that the predominant pertussis toxin substrate is immunochemically distinct from previously identified substrates, transducin, G(i), and G(o).
Scientific Publication
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