TY - JOUR
T1 - 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
AU - Pines, M.
AU - Gierschik, P.
AU - Milligan, G.
AU - Klee, W.
AU - Spiegel, A.
PY - 1985
Y1 - 1985
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0021880176&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021880176&partnerID=8YFLogxK
U2 - 10.1073/pnas.82.12.4095
DO - 10.1073/pnas.82.12.4095
M3 - Article
C2 - 3923487
AN - SCOPUS:0021880176
SN - 0027-8424
VL - 82
SP - 4095
EP - 4099
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 12
ER -