ADP-ribosylation by cholera toxin of membranes derived from brain modifies the interaction of adenylate cyclase with guanine nucleotides and NaF.
ADP-ribosylation by cholera toxin of membranes derived from brain modifies the interaction of adenylate cyclase with guanine nucleotides and NaF.
复制标题
霍乱毒素对脑膜的 ADP 核糖基化改变了腺苷酸环化酶与鸟嘌呤核苷酸和 NaF 的相互作用。
DOI：
10.1111/j.1471-4159.1988.tb02480.x
复制
发表时间：
1988
影响因子：
4.7
通讯作者：
Gill,DM
中科院分区：
文献类型：
--
作者：
Tamir,A;Gill,DM
We have developed a method to ADP‐ribosylate the stimulatory guanine nucleotide‐binding protein of adenylate cyclase (Gs) in brain membranes by using cholera toxin. In particular, we used isonicotinic acid hydrazide and 3‐acetylpyridine adenine dinucleotide to inhibit the potent NAD‐glycohydrolase activity of brain membranes, and we used the detergent Triton X‐100 (at 0.1%) to improve the accessibility of the toxin and guanine nucleotides used for supporting the ADP‐ribosylation. This method reveals that Gsis a very abundant protein in membranes derived from calf brain (∼30 pmol/mg of protein). In brain, Gsexists in large excess over the previously reported amount of the adenylate cyclase catalytic subunit. The modification of Gswith an ADP‐ribosyl residue (a) elicits a four‐ to fivefold activation of adenylate cyclase by GTP, (b) increases the stabilization of adenylate cyclase by GTP, and (c) reduces adenylate cyclase activation by fluoride but does not change basal activity, activation by guanosine5′‐(β,γ‐imido)triphosphate, or the sensitivity of adenylate cyclase to heat‐induced denaturation. A correlation between ADP‐ribosylation and the alterations in the activation of adenylate cyclase by guanine nucleotides and by fluoride is presented.
