Egg lysozyme

From crystal-structure analysis of hen-egg lysozyme and of its complex with the competitive inhibitor tri-Af-acetylchitotriose, the following conclusions were drawn the active site consists of a cleft containing six sub-sites, A to F, of which each could accommodate a) -( 1 — 4)-linked A-acetylglucosa-... 

The discrete protonation states methods have been tested in pKa calculations for several small molecules and peptides, including succinic acid [4, 25], acetic acid [93], a heptapeptide derived from ovomucoid third domain [27], and decalysine [61], However, these methods have sofar been tested on only one protein, the hen egg lysozyme [16, 61, 71], While the method using explicit solvent for both MD and MC sampling did not give quantitative agreement with experiment due to convergence difficulty [16], the results using a GB model [71] and the mixed PB/explicit... 

Machuqueiro M, Baptista AM (2007). Stochastic titration study of hen egg lysozyme. Proteins 72 289-298. 

Tanaka S, Oda Y, Ataka M, et al. Denaturation and aggregation of hen egg lysozyme in aqueous ethanol solution studies by dynamic light scattering. Biopolymers 2001 59 370-379. 

Goda S, Takano K, Yamagata Y, et al. Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution. Protein Sci. 2000 9 369-375. 

Cytochrome c peroxidase domain 1 C. Miscellaneous antiparallel a Carp muscle calcium-binding protein Egg lysozyme Citrate synthase Catalase domain 2 Cytochrome c peroxidase domain 2 p-Hydroxybenzoate hydroxylase domain 3 II. Parallel a/j3 domains... 

To test DC-specific targeting, model antigens such as hen egg lysozyme (HEL) and ovalbumin (OVA) were covalently linked to anti-DEC-205 antibodies and injected into mice. This resulted in antigen loading of the lymph node DCs,... 

Sometimes, biotinylating reagents may lose their reactivity, typically by hydrolysis of the NHS-ester moiety, it is recommended that the quality of the reagent is checked by biotinylating 1 mg hen egg lysozyme at (3.1) biotin-protein ratio. 

An even more serious disadvantage of this technique is that it often impairs the biological activity of the modified protein. The activities of hen s egg lysozyme (EC 3.2.1.17) and alpha amylase from Aspergillus oryzae (EC 3.2.1.1) were lessened by diazo coupling of glycosides or aniline.12 Whether the decrease in activity was due to the modification of critical residues, or to the introduction of aromatic structures, is not yet clear however, enzymes subjected to the diazocoupling conditions in the absence of the diazonium salts retained their activity, implying that the reaction conditions themselves were not responsible for the loss of activity. 

The harvested cells were dispersed in 100 mL of purification buffer A containing 50 mM sodium acetate (pH 5.0), 2 mMDTT, and then disrupted using lOmgofhen egg lysozyme and 15 min of sonication. 

Figure 3.18 Schematic diagram of the hen egg lysozyme refolding procedure with the help of ethane-bridged PMOs.241 (Reprinted with permission from X. Wang et al., Langmuir 2007, 23, 5735-5739. Copyright 2007 American Chemical Society.) (See color insert.)...

Kinetics of Anti-Hen Egg Lysozyme Monoclonal Antibodies Hyhel-5 and Hyhel-10. 

Elofsson M, Roy S, Walse B, Kihlberg J, Solid-phase synthesis and conformational studies of glycosylated derivatives of helper-T-cell immunogenic peptides from hen-egg lysozyme., Carbohydr. Res., 17, 246 89-103, 1993. 

Figure 6-1. Complex formed between an immunoglobulin and a hen egg lysozyme highlighting the mutated residues with a vdW representation. The null-spots are represented in yellow (relative binding energy <2.0 kcal/mol), the warm-spots in orange (relative binding energy between 2.0 and 4.0 kcal/mol), and the hot spots in red (residues with a relative binding energy higher than 4.0 kcal/mol)...

Hen egg lysozyme is a small enzyme, having a single polypeptide chain of 129 aminoacid residues and a molecular mass of approximately 14400 Da, that catalyzes the hydrolysis of glycosidic linkages in bacterial cell walls. The schematic illustration of the active sites of lysozyme is shown in Fig. 10.29. 

All of the a-lactalbumins and lysozymes studied, except the egg lysozymes, have negative bands near 270 nm. It is not possible to allocate these bands unequivocally, but they appear to involve Tyr perturbation. Differences in chirality of the disulfide bridges in a-lactalbumin and lysozyme may also cause appreciable contribution to bands in the 240- to 270-nm region. 

The curves in this region cannot be classified simply as typical of mammalian lysozymes, egg lysozymes, and a-lactalbumins. The spectra for bovine, pig, and kangaroo a-lactalbumins are very similar. On the other hand, the curve for human a-lactalbumin is similar to that for human lysozyme, but different from that of domestic hen lysozyme. The curve for echidna lysozyme I resembles that of human lysozyme fairly closely. The side-chain effects of red kangaroo a-lactalbumin and echidna lysozyme I resemble those of human lysozyme (Hopper and McKenzie, 1974). 

Figure 2. SDS gel electrophoresis of the products of partial cystine cleavage for several test proteins. A. molecular weight standards, B. yeast alcohol dehydrogenase. C. P-lactoglobulin, D. hen egg lysozyme, E. ovalbumin, F. calf fetal serum fetuin. Molecular weight standards are indicated by arrows on the left side of the gel and are bovine serum albumin (66,300), bovine liver glutamate dehydrogenase (55,400), porcine muscle lactate ddiydiogenase (36,500), bovine erythrocyte carbonic anhydrase (31,000), soybean trypsin inhibitor (21,500), hen egg lysozyme (14,400), bovine lung aprotinin (6,000), unresolved bovine pancreatic insulin A and B chains.

Useful internal sequences and useful structural information can be gathered from this technique. However, like any digestion procedure, there is no guarantee that useful information will be obtained in every case. The sequences obtained for chicken egg lysozyme (data not shown) gave amino terminal sequence for every band. Given that lysozyme is a small protein with four disulfide bands and that all but two of the eight cysteine residues are located in the C-terminal half of the molecule, this result is not surprising. 

Slagle, S., R. E. Kozack and S. Subramaniam. (1994). Role of electrostatics in antibody-antigen association anti-hen egg lysozyme/lysozyme complex (HyHEL-5/HEL). J. Biomol. Struct. Dyn. 12 439-56. 

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