Two gamma-subunits, gamma-I and gamma-II, complex with the same beta-subunits in bovine brain G-proteins (Gi/o).
When a mixture of bovine brain G-proteins (Gi/o) was loaded onto an octyl sepharose column in the presence of AlF4-, alpha-subunits of molecular weights 39 kDa and the 41 kDa were eluted separately, followed by the appearance of two distinct peaks containing beta gamma-subunits (beta gamma-I, beta gamma-II). Both beta gamma-I and beta gamma-II possessed identical beta-subunits but different gamma-subunits. The molecular weights of the two gamma-subunits determined by SDS-polyacrylamide gel electrophoresis both in the presence and absence of urea were 4.5 kDa (gamma-I) and 5.0 kDa (gamma-II). Tests indicated that the two isolated gamma-subunits are intact and have not undergone proteolysis. The amino acid composition of gamma-I appeared to be distinct from that of gamma-II. Therefore, this method is a simple procedure for isolating beta gamma-I and beta gamma-II.
Sohma
H
H
Department of Biochemistry, Sapporo Medical College, Japan.
Hashimoto
H
H
Ohguro
H
H
Akino
T
T
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001921:Brain / Q000378:metabolism*; D002417:Cattle; D002852:Chromatography, Ion Exchange; D004247:DNA / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D019204:GTP-Binding Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D046911:Macromolecular Substances; D008745:Methylation; D008970:Molecular Weight; D011485:Protein Binding; D012436:S-Adenosylmethionine / Q000378:metabolism; D014316:Tritium
D000596:Amino Acids; D046911:Macromolecular Substances; D014316:Tritium; D012436:S-Adenosylmethionine; D004247:DNA; D019204:GTP-Binding Proteins