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thaumatin/necroză

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ArticoleStudii cliniceBrevete
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Structural Characterization and Pro-inflammatory Activity of a Thaumatin-like Protein from the Pulp Tissues of Litchi chinensis.

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The objective of this study was to extract and purify proteins from the pulp tissues of litchi and evaluate their structure and pro-inflammatory activity. The results showed that a highly pure litchi protein was identified as litchi thaumatin-like protein (LcTLP) by nano LC-MS/MS and verified by
OBJECTIVE This study was conducted to determine the role of gut-derived bacteria/endotoxin in the pathogenesis of the multiple-organ damage and mortality, the possible beneficial effect of recombinant bactericidal/permeability-increasing protein (rBPl21), and whether neutralizing endotoxemia by

Cultivar-specific elicitation of barley defense reactions by the phytotoxic peptide NIP1 from Rhynchosporium secalis.

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Resistance of barley to the phytopathogenic fungus, Rhynhosporium secalis race US238.1, was found to be controlled by resistance gene Rrs1, which segregated in a manner characteristics for a codominant gene. PRHv-1, a thaumatin-like pathogenesis-related protein, was shown to be encoded by a gene
Cyclophosphamide-induced neutropenia exacerbates septic shock and multiple organ injury in conscious rats during Escherichia coli (EC) bacteremia despite antibiotics and fluid administration. We hypothesized that such shock and inflammatory organ injury would be mitigated by rBPI23's microbicidal
OBJECTIVE To investigate the role of recombinant bactericidal/permeability-increasing protein (rBPI21) in the attenuation of the sepsis syndrome and acute lung injury associated with lower limb ischemia-reperfusion (I/R) injury. BACKGROUND Gut-derived endotoxin has been implicated in the conversion

Bactericidal/permeability-increasing protein ameliorates acute lung injury in porcine endotoxemia.

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Bactericidal/permeability-increasing protein (BPI), a cationic protein isolated from human neutrophils, binds lipopolysaccharide (LPS), kills gram-negative bacteria, and neutralizes many of the effects of LPS in vitro and in vivo. We hypothesized that a recombinant 23-kDa NH2-terminal fragment of
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