The antibody raised against an aminoacidic sequence that is conserved among many animal G protein ? subunits (anti-? common antibody) recognized some membrane proteins from rice coleoptile on immunoblot. Two of them, showing apparent molecular weights of 28 and 30 kDa, dissociated from aerobic and anoxic coleoptile membranes following GTP?S or GTP stimulation, but not after GDP addition. Furthermore, anti-? common antibody could be used to immunoprecipitate a saturable GTP binding activity from the supernatant of [35S]GTP?S-stimulated membranes, but not after [3H]GDP addition
Two putative G-protein alpha subunits dissociate from both aerobic and anoxic rice (O. sativa L.) coleoptile membranes after GTP stimulation.
Diego Breviario;Sergio Mapelli;Remo Reggiani
1994
Abstract
The antibody raised against an aminoacidic sequence that is conserved among many animal G protein ? subunits (anti-? common antibody) recognized some membrane proteins from rice coleoptile on immunoblot. Two of them, showing apparent molecular weights of 28 and 30 kDa, dissociated from aerobic and anoxic coleoptile membranes following GTP?S or GTP stimulation, but not after GDP addition. Furthermore, anti-? common antibody could be used to immunoprecipitate a saturable GTP binding activity from the supernatant of [35S]GTP?S-stimulated membranes, but not after [3H]GDP additionFile in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
