Purification of Cysteine-Rich Bioactive Peptides from Leukocytes by Continuous Acid-Urea-Polyacrylamide Gel Electrophoresis
✍ Scribed by S.S.L. Harwig; N.P. Chen; A.S.K. Park; R.I. Lehrer
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 463 KB
- Volume
- 208
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
A new continuous acid-urea-polyacrylamide gel electrophoresis (CAU-PAGE) preparative method was developed and used to purify rabbit and human defensins. With it, we identified two post-translationally modified forms of rabbit defensins NP-1 and NP-2, and purified a processed RANTES ( (\beta)-intercrine) peptide from leukophoresed human leukocytes. CAU-PAGE afforded approximately (70 %) recovery of rabbit defensin NP-5. The recovered defensins were not (\mathrm{N})-terminally modified, and their in vitro antimicrobial activity was equivalent to that of defensins purified by previously described chromatographic methods. Since CAU-PAGE is performed under nonreducing conditions, it should be especially useful for purifying cationic peptides with intramolecular disulfide bonds, such as defensins and (\alpha) or (\beta)-intercrines. cc 1993 Academic Press, Inc.