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Hen 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-... [Pg.325]

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... [Pg.269]

Machuqueiro M, Baptista AM (2007). Stochastic titration study of hen egg lysozyme. Proteins 72 289-298. [Pg.282]

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. [Pg.283]

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. [Pg.283]

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,... [Pg.30]

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. [Pg.495]

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.)... 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. [Pg.93]

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. [Pg.53]

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)... 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. [Pg.819]

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. 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.
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. [Pg.234]

Tani, F. et al., Heat-induced transparent gel from hen egg lysozyme by a two-step heating method, Biosci. Biotech. Biochem., 57, 209, 1993. [Pg.177]

Fig. 20. Primary structure of hen-egg lysozyme. ALA alanine, ARG arginine, ASN asparagine, ASP aspartic acid, CYS cysteine, GLN glutamine, GLU glutamic acid, GLY glycine, HIS histidine, ILE isoleucine, LEU leucine, LYS lysine, MET methionine, PHE phenylalanine, PRO proline, SER serine, THR threonine, TRP tryptophan, TYR tyrosine, VAL valine. (Redrawn from Canfield and Lu, 1965). Fig. 20. Primary structure of hen-egg lysozyme. ALA alanine, ARG arginine, ASN asparagine, ASP aspartic acid, CYS cysteine, GLN glutamine, GLU glutamic acid, GLY glycine, HIS histidine, ILE isoleucine, LEU leucine, LYS lysine, MET methionine, PHE phenylalanine, PRO proline, SER serine, THR threonine, TRP tryptophan, TYR tyrosine, VAL valine. (Redrawn from Canfield and Lu, 1965).
A set of hybrid proteins containing the Ap40 peptide domain and dimeric glucose dehydrogenase (GDH) or thioredoxin (Trx) have been constructed in present work. Expression and purification of the proteins was accomplished using prokaryotic system based on Escherichia coli. Details of the construction and expression of hybrid proteins are subject of special report and will be presented elsewhere. Hen egg lysozyme was fibrilized as described in our recent work. [Pg.65]

Self assemblage of extended biomolecular structures on solid surfaces was verified by the SPM measurements. Supramolecular structures were detected on solid surfaces of practically all samples. Aiming to characterize transferability of the structures from the solution onto solid surface, we performed experiments with sufficiently stable lisozyme fibrils. In these experiments hen egg lysozyme fibrils were immobilized on several types of solid substrates listed in section 2 by deposition of the structures from buffer solution. Typical results of these tests are... [Pg.65]

It was proved experimentally that immobilization period can be effectively used for variation of the density of the supramolecular structures on the surfaces. Influence of the immobilization time on die arrangement of the combined structures is illustrated in Fig. 2 by typical SPM images obtained for hen egg lysozyme fibrils deposited on mica surfaces. After deposition of the lysozyme fibrils under similar conditions, the fibrils were rare on the surfaces if immobilization was shorter... [Pg.66]

Figure 3 shows typical binding isotherms for hen egg lysozyme on binding sodium n-dodecylsulphate (SDS) in acid solution, pH 3.2, 25°C. Lysozyme (molecular mass 14,306) has a single polypeptide chain with an /V-terminal lysine residue, four disulphide bonds, and 18 cationic residues (11 arginyl, 6 lysyl, and 1 histidyl). At very low free SDS concentrations the binding isotherms are very steep but... [Pg.245]

Hibbits, K. A., Gill, D. S., and Willson, R. C. (1994). Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL-5. Biochemistry 33(12), 3584-3590. [Pg.69]

AltobelH, G., Subramaniam, S. Kinetics of association of anti-lysozyme monoclonal antibody D44.1 and hen-egg lysozyme. Biophys. J. 2000, 79,2954-65. [Pg.86]

Stir suspension in a shearing mixer such as a blender at top speed for 1 min. Add hen egg lysozyme (100 mg) to the suspension and stir overnight at 4°C. [Pg.5]


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See also in sourсe #XX -- [ Pg.403 ]




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