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
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发表时间:
1984
期刊:
影响因子:
2.9
通讯作者:
Nicholas,RA
中科院分区:
文献类型:
--
作者:
Nicholas,RA
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