Lysozyme chicken

Use of the anionic CP allowed for detection of amyloid fibril formation in both bovine insulin and chicken lysozyme proteins (Fig. 16). The polymer in buffer... 

Amino Acid Group Average Protein Chicken lysozyme... 

Figure 12.9. Protein structure prediction with PHD. The amino acid sequence of chicken lysozyme precursor (147 amino acids) is submitted to PredictProtein server for PHD structure predictions. The returned e-mail reports protein class based on secondary structures, predicted secondary structure composition (%H, %E, and %L), residue composition, data interpretation, and predicted data in two levels (brief and normal of which the normal is shown). Search for the database can be performed by making choice(s) from the list(s) of pop-up box(es).

Figure 14.12. Superimposition of molecular structures with HyperChem. Pigeon lysozyme structure (red) derived from homology modeling with Swiss-PDB Viewer is overlapped against chicken lysozyme structure, pdb1 lyz.ent (black). Two catalytic residues, Glu35 and Asp 52 (chicken lysozyme), are highlighted (green).

Chicken lysozyme P-lactoglobulin A P-lactoglobulin B rabbit parvalbumin hcc, hhm Open-tubular UV 28... 

It has now been found that the glucocorticoid response elements of mouse mammary tumour virus and the gene for chicken lysozyme also bind progesterone re-... 

Subcloning into Yeast Expression Vector. Mutant chicken lysozyme sequences located in a 2.5-kilobase (kb) BamHl fragment are subcloned into the Bam HI site of the yeast shuttle plasmid pAB2413 according to the procedure of Gibco BRL Life Technologies, Inc., Grand Island, NY. This... 

Protein Production, Isolation, and Purification. The expression and purification of chicken lysozyme mutant proteins in yeast are performed as described by Malcolm et al. with the following modifications. The 50-ml minimal medium second seed yeast culture is used to inoculate a 2.8-liter Fembach flask containing 500 ml of 1% yeast extract/2% Bacto-peptone/ 8% glucose (w/v) medium and is then incubated for 7 - 9 days at 30°. Cells are harvested, washed twice with 60 ml of 0.5 M NaCl, and collected by centrifugation. The supernatants are pooled, diluted 5-fold with deionized water, and loaded onto a 20-ml column of CM Sepharose Fast Flow (Pharmacia, Piscataway, NJ) equilibrated with 0.1 M potassium phosphate, pH 6.24. The column is washed with the same buffer, and lysozyme is eluted with 0.5 M NaCl/0.1 M potassium phosphate, pH 6.24. Fractions are assayed by activity (decrease in A450 of Micrococcus lysodeikticus cell wall suspensions per minute). Fractions containing lysozyme are concentrated in Centricon-10 (Amicon, Danvers, MA) filter units, washed with 0.1 M potassium phosphate buffer, pH 6.24, and stored at 4°. The protein concentration is determined from e 1 = 26.4.15... 

The objective of the experiments is to compare the affinity of wild-type antibody and wild-type immunogen (chicken lysozyme) with that of wild-type antibody and mutant antigen or with that of mutant antibody and wild-type immunogen. All the assays involve incubation of a constant concentration of one reactant with varying amounts of the complementary reactant, along with estimating the concentration of either bound or free reactant by an immunochemical or enzymatic method. In each case, the assumption is made that the measurement step does not disturb the equilibrium between antigen and antibody, and it is important that this assumption be validated experimentally. We summarize below several alternative methods. 

Fig. 1. Effect of HyHEL-10 on M. lysodeikticus lysis activity of chicken lysozyme at 0.1 nM concentration using the competitive inhibition enzyme assay described in the text (a) Raw data with varying concentrations of antibody and the substrate-only control, (b) Plot of antibody concentration versus decrease in absorbance at 450 nm per minute at 0.1 nAf enzyme (unconected for substrate-only control).

Chicken lysozyme residue Asp-lOlma in the HyHEL-10 epitope7 is of additional interest because it contributes to the free energy of association of substrate ligands with the enzyme 33 turkey lysozyme (TEL) has a glycine at position 101.34 Nine replacements were designed to test the importance... 

Bovine proalbumin Mouse antibody H chain Chicken lysozyme Bee promellitin Drosophila glue protein Zea maize protein 19 Yeast invertase Human influenza virus A... 

Phi-Van, L., von Kries, J.P., Ostertag, W, and Stratling, W. H. (1990) The chicken lysozyme 5 matrix attachment region increases transcription from a heterologous promoter in heterologous cells and dampens position ef fects on the expression of transfected genes. Mol. Cell. Biol. 10 2302-2307. 

GeuBank (upper) and EMBL (lower) formats for nucleotide sequence of chicken lysozyme gene... 

Baniahmad, A., Muller, M., Sterner, C. Renkawitz, R. (1987). Activity of two different silertcer elements of the chicken lysozyme gene can be expressed by enhancer elements. EMBO ]., 6, 2297-303. 

Baniahmad, A., Steiner, C., Kohne, A.C. Renkawitz, R. (1990). Modular structure of a chicken lysozyme silencer involvement of an unusual thyroid hormone receptor biiKling site. 

Bonifer, C., Vidal, M., Grosveld, F. Sippel, A.E. (1990). Tissue specific and position independent expression of the complete domain for chicken lysozyme in transgenic mice. EMBO ]., 9, 2843-8. 

Dolle, A. Stratling, W.H. (1990). Genomic footprinting of proteins interacting with the chicken lysozyme promoter. Gene 95, 187-93. 

Grewal, T., Thiesea M., Borgmeyer, U. et al (1992). The —6.1-kilobase chicken lysozyme enhatKer is a multifactorial complex containing several cell-type-specific elements. Mol. all Biol, 12, 2339-50. 

Hecht, A., Berkenstamm, A., Stromstedt, P.-E., Gustaksoa J -A. Sippel, A.E. (1988). A progesterone responsive element maps to the far upstream steroid dependent DNAse hypersensitive site of the chicken lysozyme chromatin. EMBO ]., 7, 2063-73. 

Quasba, P.K. Safaya, S.K. (1984). Similarity of the nucleotide sequences of rat a-lactalbumin and chicken lysozyme genes. Nature, 308, 377-80. 

The polymer P2.209 was used as an optical probe in the detection of amyloid fibril formation of bovine insulin (BI) and chicken lysozyme in acetic acid medium. Upon interaction with BI, a drastic increase... 

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