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פותח על ידי קלירמאש פתרונות בע"מ -
Antibodies against the carboxyl-terminal 5-kDa peptide of the α subunit of transducin crossreact with the 40-kDa but not the 39-kDa guanine nucleotide binding protein from brain
Year:
1985
Authors :
פינס, מרק
;
.
Volume :
82
Co-Authors:
Pines, M., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Gierschik, P., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Milligan, G., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Klee, W.
Spiegel, A.
Facilitators :
From page:
4095
To page:
4099
(
Total pages:
5
)
Abstract:
We tested 18 antisera showing reactivity against the α subunit of transducin, the guanine nucleotide binding protein from rod outer segment, for crossreactivity against the 40- and 39-kDa guanine nucleotide binding proteins purified from bovine brain. A single antiserum, CW6, showed crossreactivity, and this was predominantly against the 40-kDa protein. Immunoblots of the tryptic fragments of transducin α subunit with multiple antisera raised against that subunit showed that only CW6 recognizes a COOH-terminal 5-kDa peptide that includes the site of pertussis toxin ADP-ribosylation. Antibodies against the 5-kDa peptide, affinity-purified from CW6, specifically react with the 40-kDa brain protein on immunoblots. The results show that the 39- and 40-kDa guanine nucleotide binding proteins from brain differ immunochemically and that the COOH-terminal 5-kDa peptide of transducin α subunit is homologous to a region in the 40-kDa brain protein. We speculate that this homologous region may be in a domain that confers specificity for receptor interactions of guanine nucleotide binding proteins.
Note:
Related Files :
animal cell
Animals
cattle
Macromolecular Substances
Mammalia
Peptide Fragments
protein 5k
unclassified drug
visual system
עוד תגיות
תוכן קשור
More details
DOI :
10.1073/pnas.82.12.4095
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
26110
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:20
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Scientific Publication
Antibodies against the carboxyl-terminal 5-kDa peptide of the α subunit of transducin crossreact with the 40-kDa but not the 39-kDa guanine nucleotide binding protein from brain
82
Pines, M., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Gierschik, P., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Milligan, G., Metabolic Diseases Branch, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20205, United States
Klee, W.
Spiegel, A.
Antibodies against the carboxyl-terminal 5-kDa peptide of the α subunit of transducin crossreact with the 40-kDa but not the 39-kDa guanine nucleotide binding protein from brain
We tested 18 antisera showing reactivity against the α subunit of transducin, the guanine nucleotide binding protein from rod outer segment, for crossreactivity against the 40- and 39-kDa guanine nucleotide binding proteins purified from bovine brain. A single antiserum, CW6, showed crossreactivity, and this was predominantly against the 40-kDa protein. Immunoblots of the tryptic fragments of transducin α subunit with multiple antisera raised against that subunit showed that only CW6 recognizes a COOH-terminal 5-kDa peptide that includes the site of pertussis toxin ADP-ribosylation. Antibodies against the 5-kDa peptide, affinity-purified from CW6, specifically react with the 40-kDa brain protein on immunoblots. The results show that the 39- and 40-kDa guanine nucleotide binding proteins from brain differ immunochemically and that the COOH-terminal 5-kDa peptide of transducin α subunit is homologous to a region in the 40-kDa brain protein. We speculate that this homologous region may be in a domain that confers specificity for receptor interactions of guanine nucleotide binding proteins.
Scientific Publication
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