PURIFICATION AND CHARACTERIZATION OF ADENYLATE CYCLASE
PURIFICATION AND CHARACTERIZATION OF ADENYLATE CYCLASE
批准号:
3400844
负责人:
DANIEL R STORM
金额:
$12.24万
依托单位:
依托单位国家:
美国
项目类别:
财政年份:
1984
资助国家:
美国
项目状态:
已结题
起止时间:
1984-04-01 至 1995-03-31
关键词:
adenosine triphosphate adenylate cyclase affinity chromatography antibody beta adrenergic receptor brain calcium calmodulin complementary DNA cyclic AMP enzyme inhibitors enzyme mechanism enzyme reconstitution enzyme structure fluorescence spectrometry genetic manipulation isoproterenol laboratory mouse laboratory rabbit membrane proteins molecular cloning protein kinase protein kinase A protein kinase C
中文摘要
细胞内cAMP控制多环芳烃、脂质、蛋白质
以及动物细胞中的核酸代谢。 辅酶A,cAMP
在几种神经元功能中起着重要作用
包括突触传递和特定离子的活性
通道由cAMP调节。大脑中的cAMP水平为
由腺苷酸环化酶直接控制,腺苷酸环化酶由
神经递质和Ca2+。 这一长期目标
该项目旨在阐明大脑的调节机制,
腺苷酸环化酶,钙调素和cAMP依赖蛋白
激酶。 我们的实验室最近提纯了这种酶,
同源性和获得的多克隆抗体对钙调素
敏感腺苷酸环化酶。 而且我们
最近发现了一种来自大脑的蛋白质,命名为pp90,
激活脑腺苷酸环化酶,我们怀疑这是一种
钙结合蛋白 该项目的具体目标包括:
牛脑钙调素敏感性腺苷酸环化酶的纯化
使用免疫亲和层析,纯化CaM
敏感的腺苷酸环化酶,钙调素的检查,
钙调素敏感性腺苷酸的钙敏感性和异丙肾上腺素敏感性
用β肾上腺素能受体重建环化酶,和
阐明酶的调节机制,
cAMP依赖性蛋白激酶。 此外,我们建议
阐明腺苷酸环化酶的调节机制,
pp90. 我们还将尝试克隆编码
CaM敏感腺苷酸催化底物的序列
牛脑环化酶。 该项目将提供
关于腺苷酸结构的基本信息
环化酶和调节酶的机制,
Ca2+、蛋白激酶和儿茶酚胺。
英文摘要
Intracelluar cAMP controls aspects of carbolydrate, lipid, protein
and nucleic acid metabolism in animal cells. Futhermore, cAMP
plays an important role for several types of neuronal function
including synaptic transmission, and the activity of specific ion
channels is regulated by cAMP. The levels of cAMP in brain are
directly controlled by adenylate cyclase which is regulated by
neurotransmitters and Ca2+. The long-term objectives of this
project are to elucidate the mechanisms for regulation of brain
adenylate cyclase by Ca2+, CaM, and cAMP dependent protein
kinase. Our laboratory has recently purified this enzyme to
homogeneity and obtained polyclonal antibodies against the CaM
sensitive adenylate cyclase front bovine brain. Furthermore, we
have recently discovered a protein from brain, designated pp90,
that activates brain adenylate cyclase which we suspect is a
calcium binding protein. Specific aims of this project include the
purification of CaM sensitive adenylate cyclase from bovine brain
using immunoaffinity chromatography, purification of the CaM
sensitive adenylate cyclase from brain, examination of the CaM,
Ca2+, and isoproterenol sensitivity of the CaM sensitive adenylate
cyclase reconstituted with beta adrenergic receptors, and
elucidation of the mechanism for regulation of the enzyme by
cAMP dependent protein kinase. Furthermore, we propose to
elucidate the mechanism for regulation of adenylate cyclase by
pp90. We will also attempt to clone cDNA's encoding the
sequence of the catalytic submit of the CaM sensitive adenylate
cyclase from bovine brain. This project should provide
fundemental information concerning the structure of adenylate
cyclases and the mechanisms for regulation of the enzyme by
Ca2+, protein kinases, and catecholamines.
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