Separation of limited tryptic fragments of human ceruloplasmin by gel-permeation high-performance liquid chromatography.


Journal Article

Limited tryptic proteolysis of human ceruloplasmin rapidly produces several large, protease-resistant fragments, suggesting that the molecule consists of several domains. In order to locate the sites of proteolytic cleavage in the whole molecule, we used gel-permeation high-performance liquid chromatography to determine the optimum conditions for fragment separation. Using a buffer containing 8 M urea, the 67,000-daltons tryptic fragment from single-chain ceruloplasmin was isolated in a sufficiently pure state for amino acid sequence analysis to determine its location in the uncleaved molecule. These results have been used in conjunction with amino acid sequence data to develop a schematic model of the domain structure of human ceruloplasmin.

Full Text

Duke Authors

Cited Authors

  • Ortel, TL; Takahashi, N; Putnam, FW

Published Date

  • August 26, 1983

Published In

  • J Chromatogr

Volume / Issue

  • 266 /

Start / End Page

  • 257 - 263

PubMed ID

  • 6630352

Pubmed Central ID

  • 6630352

Digital Object Identifier (DOI)

  • 10.1016/s0021-9673(01)90899-4


  • eng

Conference Location

  • Netherlands