Reduced, denatured lysozyme tends to aggregate at neutral pH, and competition between productive folding and aggregation substantially reduces the efficiency of refolding (Goldberg, M.E., Rudolph, R., and Jaenicke, R. (1991) Biochemistry 30, 2790-2797). Protein disulfide isomerase (PDI), a catalyst of oxidative protein folding, has a variety of effects on the yield of native lysozyme during the...

Oxidative refolding of the denatured/reduced lysozyme was examined in the presence of small unilamellar vesicles (SUVs) essentially composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC). SUVs facilitated the recovery of the enzymatic activity of lysozyme like molecular chaperones through the interaction with the refolding intermediate of lysozyme. The highest reactivation yield (8...

Lysozymes are key effectors of the animal innate immunity system that kill bacteria by hydrolyzing peptidoglycan, their major cell wall constituent. Recently, specific inhibitors of the three major lysozyme families occuring in the animal kingdom (c-, g- and i-type) have been discovered in Gram-negative bacteria, and it has been proposed that these may help bacteria to evade lysozyme mediated l...

Listeria monocytogenes is a Gram-positive facultative intracellular pathogen that is highly resistant to lysozyme, a ubiquitous enzyme of the innate immune system that degrades cell wall peptidoglycan. Two peptidoglycan-modifying enzymes, PgdA and OatA, confer lysozyme resistance on L. monocytogenes; however, these enzymes are also conserved among lysozyme-sensitive nonpathogens. We sought to i...

Rabbit tear lysozyme was detected in low concentration in rabbit tears collected without any stimulation. Quantitation of rabbit tear lysozyme was found possible through the use of sensitive techniques that measure its specific enzymic activity on the bacterial cell walls of Micrococcus lysodeikticus. Rabbit tear lysozyme has an electrophoretic mobility identical to that of hen egg-white lysozy...

Lysozyme is a globular protein which is known to bind to negatively charged phospholipid vesicles. In order to study the relationship between binding of the protein and the subsequent destabilization of the phospholipid vesicles a set of experiments was performed using phospholipid monolayers and vesicles. Using microelectrophoresis the binding of lysozyme to phospholipid vesicles made of PS wa...

Lysozyme turnover in the rat was studied with (125)I-labeled rat lysozyme. It was found that plasma lysozyme has a rapid disappearance rate with a half-life of 75 min. The rate of synthesis was calculated at 3.4 mug/min per 100 g rat. This rate of synthesis was compared with figures from the literature for the turnover rate of neutrophilic granulocytes, and the data were consistent with the con...

Direct evidence has been obtained that the tail-associated lysozyme of bacteriophage T4 (tail-lysozyme) is gp5, which is a protein component of the hub of the baseplate. Tails were treated with 3 M guanidine hydrochloride containing 1% Triton X-100, and the tail-lysozyme was separated from other tail components by preparative isoelectric focusing electrophoresis as a peak with a pI of 8.4. The ...

Lysozyme was attached to three cotton fabrics through a glycine amino acid linker esterifi ed to cotton cellulose. Lysozyme bound to cotton twill using a carbodiimide-mediated coupling reaction gave the best lysozyme incorporation (16.1 mg/g of cotton). Cotton spunlace nonwoven fabric bound slightly less lysozyme (12.8 mg/g of cotton), but had the best antimicrobial activity. Woven print cloth ...