Purification of the membrane-spanning tryptic peptides of the alpha polypeptide from sodium and potassium ion activated adenosinetriphosphatase labeled with 1-tritiospiro[adamantane-4,3'-diazirine].

Purification of the membrane-spanning tryptic peptides of the alpha polypeptide from sodium and potassium ion activated adenosinetriphosphatase labeled with 1-tritiospiro[adamantane-4,3'-diazirine].
复制标题

从用 1-tritiospiro[adamantane-4,3-diazirine] 标记的钠离子和钾离子激活的腺苷三磷酸酶中纯化 α 多肽的跨膜胰蛋白酶肽。

DOI:
10.1021/bi00300a015
复制
发表时间:
1984
期刊:
影响因子:
2.9
通讯作者:
Nicholas,RA
Nicholas,RA
中科院分区:
生物学3区
文献类型:
--
作者:
Nicholas,RA

文献摘要

相似文献

Robert A.尼古拉斯摘要:从钠、钾离子激活的腺苷三磷酸酶[(Na ~++ K ~+)-ATP酶]的多肽中纯化了五个长的跨膜胰蛋白酶肽。(Na从犬肾中分离的(++ K+)-ATP酶在高浓度1-tritiospiro [金刚烷-4,3 '-diazirine]存在下暴露于紫外光,1-tritiospiro [金刚烷-4,3'-diazirine]是一种分配到膜双层中的卡宾前体。分离用1.2mol [3 H]金刚烷亚基(mol多肽)1修饰的α多肽并用胰蛋白酶消化。用胰蛋白酶消化可确保跨膜序列在消化过程中保持完整,因为赖氨酸和精氨酸具有极强的亲水性,很少出现在膜蛋白的膜包埋区域。这种消化产生了放射性胰蛋白酶
Robert A. Nicholas abstract: Five long, membrane-spanning tryptic peptides from the a polypeptide of sodium and potassium ion activated adenosinetriphosphatase [(Na++ K+)-ATPase] have been purified.(Na++ K+)-ATPase, isolated from canine kidney, was exposed to ultraviolet light in the presence of a high concentration of 1-tritiospiro [adamantane-4, 3'-diazirine], a carbene precursor that partitions into the bilayer of the membrane. The a polypeptide, modified with 1.2 mol of [3H] adamantylidene (mol of polypeptide)" 1, was isolated and digested with trypsin. Digestion with trypsin ensures that membrane-spanning sequences remain intact during the di-gestion, since lysine and arginine, being extremely hydrophilic, rarely appear in the membrane-embedded regions of mem-brane proteins. This digestion produced radioactive tryptic