Zinc in Erythrocyte Ghosts

Milos Chvapil, David Montgomery, Janet C. Ludwig, Charles F. Zukoski

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


Proteins and phospholipids but not zinc were released into the medium containing hemoglobin-free ghosts from dog erythrocytes incubated in peroxidation-inducing agents (ascorbic acid, Fe2+, O2). The content of zinc in the pure ghost depends on the purification procedure; using phosphate buffer it amounted to 62 ± 22 μg/g protein, and using barbital buffer-extracted ghost it was three times higher. Although most of the zinc was linked to the lipid phase of the membrane, there is a certain protein moiety of membrane proteins binding more zinc than the other protein fractions. Among various fractions of lipids, zinc is linked mainly to phospholipids and this linkage is not broken by phosphate buffer. It is concluded that zinc is part of the erythrocyte ghost, linked to protein as well as lipid phase. This work is supported in part by NIH Research Grants AM 16489, ES 00790, and ES 01570. The professional assistance of Mrs. Waltraud W. Nichols is highly appreciated.

Original languageEnglish (US)
Pages (from-to)480-484
Number of pages5
JournalProceedings of the Society for Experimental Biology and Medicine
Issue number3
StatePublished - Dec 1979

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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