eNAP-2, a novel cysteine-rich bactericidal peptide from equine leukocytes
نویسندگان
چکیده
منابع مشابه
Identification of eNAP-1, an antimicrobial peptide from equine neutrophils.
Endogenous, cysteine-rich antimicrobial peptides known as defensins are prominent components of human, rabbit, and rat neutrophils, yet little is known about their occurrence in other mammalian species. Although we did not detect mature (i.e., processed) defensins in equine neutrophil granules, we found that these granules contained small amounts of other cysteine-rich peptides with antimicrobi...
متن کاملSelective inhibition of microbial serine proteases by eNAP-2, an antimicrobial peptide from equine neutrophils.
Equine neutrophil antimicrobial peptide 2 (eNAP-2), a recently described antimicrobial peptide isolated from equine neutrophils, was found to selectively inactivate microbial serine proteases (subtilisin A and proteinase K) without inhibiting mammalian serine proteases (human neutrophil elastase, human cathepsin G, and bovine pancreatic trypsin). Although the primary structure of eNAP-2 resembl...
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Background: Recombinant proteins overexpressed in E. coli are usually deposited in inclusion bodies. Cysteines in the protein contribute to this process. Inter- and intra- molecular disulfide bonds in chitinase, a cysteine-rich protein, cause aggregation when the recombinant protein is overexpressed in E. coli. Hence, aggregated proteins should be solubilized and allowed to refold to obtain nat...
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Sephadex G-100 chromatographic fractions of granule extracts from normal human polymorphonuclear leukocytes, exhibiting differences from fractions previously obtained from leukemic polymorphonuclear leukocytes, possessed cationic proteins with distinct bactericidal activity against cell wall mutants of Salmonella typhimurium LT2.
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Disulfide-rich peptide venoms from animals such as snakes, spiders, scorpions, and certain marine snails represent one of nature's great diversity libraries of bioactive molecules. The various species of marine cone shells have alone been estimated to produce >50,000 distinct peptide venoms. These peptides have stimulated considerable interest because of their ability to potently alter the func...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1992
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.60.12.5042-5047.1992