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

Publication ,  Journal Article
Ortel, TL; Takahashi, N; Putnam, FW
Published in: J Chromatogr
August 26, 1983

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.

Duke Scholars

Published In

J Chromatogr

DOI

Publication Date

August 26, 1983

Volume

266

Start / End Page

257 / 263

Location

Netherlands

Related Subject Headings

  • Trypsin
  • Peptide Fragments
  • Models, Structural
  • Humans
  • Chromatography, High Pressure Liquid
  • Ceruloplasmin
  • Analytical Chemistry
  • 40 Engineering
  • 34 Chemical sciences
  • 10 Technology
 

Citation

APA
Chicago
ICMJE
MLA
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Ortel, T. L., Takahashi, N., & Putnam, F. W. (1983). Separation of limited tryptic fragments of human ceruloplasmin by gel-permeation high-performance liquid chromatography. J Chromatogr, 266, 257–263. https://doi.org/10.1016/s0021-9673(01)90899-4
Ortel, T. L., N. Takahashi, and F. W. Putnam. “Separation of limited tryptic fragments of human ceruloplasmin by gel-permeation high-performance liquid chromatography.J Chromatogr 266 (August 26, 1983): 257–63. https://doi.org/10.1016/s0021-9673(01)90899-4.
Ortel, T. L., et al. “Separation of limited tryptic fragments of human ceruloplasmin by gel-permeation high-performance liquid chromatography.J Chromatogr, vol. 266, Aug. 1983, pp. 257–63. Pubmed, doi:10.1016/s0021-9673(01)90899-4.

Published In

J Chromatogr

DOI

Publication Date

August 26, 1983

Volume

266

Start / End Page

257 / 263

Location

Netherlands

Related Subject Headings

  • Trypsin
  • Peptide Fragments
  • Models, Structural
  • Humans
  • Chromatography, High Pressure Liquid
  • Ceruloplasmin
  • Analytical Chemistry
  • 40 Engineering
  • 34 Chemical sciences
  • 10 Technology