CHARACTERIZATION OF THE 2 SIZE FORMS OF THE ALPHA-1 SUBUNIT OF SKELETAL-MUSCLE L-TYPE CALCIUM CHANNELS
CHARACTERIZATION OF THE 2 SIZE FORMS OF THE ALPHA-1 SUBUNIT OF SKELETAL-MUSCLE L-TYPE CALCIUM CHANNELS
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DOI：
10.1073/pnas.88.23.10778
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发表时间：
1991-12-01
影响因子：
11.1
通讯作者：
CATTERALL, WA
中科院分区：
文献类型：
--
作者：
DEJONGH, KS;WARNER, C;CATTERALL, WA
分析了纯化的骨骼肌钙通道α 1亚基的两种大小形式的分子特性。通过Ferguson图分析，发现次要全长形式α-1（212）的表观分子量为214 kDa，而主要截短形式（现命名为α-1（190））的表观分子量为193 kDa。α-1（190）的C端区域的抗体图谱，10种抗肽抗体将C端置于残基1685和1699之间。cAMP依赖性蛋白磷酸化的三个共有位点存在于α-1（212）的C-末端区域，但不存在于α-1（190），它们可能对钙通道的离子电导活性的调节很重要。
The molecular properties of two size forms of the alpha-1 subunit of purified skeletal muscle calcium channels were analyzed. The minor, full-length, form, alpha-1(212), was found to have an apparent molecular mass of 214 kDa by Ferguson plot analysis, while the major, truncated, form, now designated alpha-1(190), had an apparent molecular mass of 193 kDa. Antibody mapping of the C-terminal region of alpha-1(190) with 10 anti-peptide antibodies placed the C terminus between residues 1685 and 1699. Three consensus sites for cAMP-dependent protein phosphorylation are present in the C-terminal region of alpha-1(212) but not in alpha-1(190), and they may be important for the regulation of the ion conductance activity of the calcium channel.