A protein with lytic activity against Micrococcus luteus was purified from the hemolymph of the fall webworm, Hyphantria cunea, larvae challenged with live E. coli. A bacteriolytic protein of about 14,000 daltons in mass was purified by cation exchange chromatography and reverse-phased HPLC. The opt
โฆ LIBER โฆ
Protein purification and cDNA cloning of a cecropin-like peptide from the larvae of fall webworm (Hyphantria cunea)
โ Scribed by Soon Sik Park; Sang Woon Shin; Doo-Sang Park; Hyun Woo Oh; Kyung Saeng Boo; Ho-Yong Park
- Book ID
- 117673499
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 557 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0965-1748
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