Identification of thiol groups and a disulfide crosslink site in bovine myelin proteolipid protein

Shyh Yu Shaw, Richard A. Laursen, Marjorie B. Lees

研究成果: Article同行評審

9 引文 斯高帕斯(Scopus)

摘要

The existence of disulfide crosslinks limits the number of possible folded structures a protein can assume. Thus localization of disulfide and thiol groups is a key to understanding the conformation and orientation of myelin proteolipid protein (PLP) in the myelin membrane. [14C]Carboxamidomethylated PLP was fragmented with chymotrypsin, and the resulting mixture was partially separated by reversed-phase HPLC. Purified 14C-labeled peptides and a disulfide containing peptide were characterized by amino acid analysis. These experiments showed that Cys-32 and Cys-34 are free thiols, and are presumably on the interior of the cell or within the membrane bilayer, and that Cys-200 and Cys-219 are joined by a disulfide bond, and are probably located on the extracellular face of the membrane. Sequence analysis experiments indicate that Cys-5, Cys-6 and Cys-9 are linked by disulfides, probably to other parts of the protein on the extracellular face of the membrane.

原文English
頁(從 - 到)306-310
頁數5
期刊FEBS Letters
250
發行號2
DOIs
出版狀態Published - 1989 7月 3

All Science Journal Classification (ASJC) codes

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 分子生物學
  • 遺傳學
  • 細胞生物學

指紋

深入研究「Identification of thiol groups and a disulfide crosslink site in bovine myelin proteolipid protein」主題。共同形成了獨特的指紋。

引用此