Lysozyme INDEX

Each set of coordinates deposited with the PDB becomes a separate entry. Each entry is associated with an accession PDB code with a unique set of four alphanumeric characters. PDB and its mirror sites offer a text search engine that uses an index of all the textual information in each PDB record (e.g., PDB ID) an example of such an index is 1LYZ for hen s egg-white lysozyme. The first character is a version number. An identifier beginning with the number 0 signifies that the entry is purely bibliographic. The pdb file is a text file with an explanatory header followed by a set of atomic coordinates. The atomic coordinates are subjected to a set of standard stereochemical checks and are translated into a standard entry format for example, Figure 4.10 shows partial coordinate file for ILYZ.pdb or pdblLYZ.ent. 

Clinical analysis of the tear film has become increasingly more developed. Examples include tear osmolarity, tear function index, and tear protein analysis, including lactoferrin, lysozyme, albumin, and immunoglobulin.Tear osmolarity and lactoferrin concentration measurements, in particular, appear to have a reliable positive predictive value among dry eye patients. At this time these techniques have more application in research than in clinical practice. 

For evaluation of tubular proteinuria, one may use either a 24-hour specimen or a random specimen. In the latter case, the concentrations of both creatinine and the specific protein (e.g., lysozyme) are determined and the protein-creatinine index is calculated as follows ... 

In nature, bovine serum albumin has a unique surface activity as compared to lysozime. The former is much more hydrophobic, having a relative hydrophobicity index (based on the fluorescence method) of 100, compared to 7 for lysozyme [1,2]. 

Figure 1 Relationships of S with interfacial tension and emulsifying activity of proteins. I, bovine serum albumin 2, /3-lactoglobulin 3. trypsin 4, ovalbumin 5, conalbuntin 6, lysozyme 7, K-casein 8, 9, I0, II, and 12, denatured ovalbumin by heating at 85°C for l, 2, 3, 4, and 5 min respectively 13, 14, 15, 16. 17, and 18. denatured lysozyme by heating at 85"C for l, 2, 3, 4, 5, and 6 min respectively 19, 20, 21, 22, and 23, ovalbumin bound with 0.2, 0.3, 1.7, 5.7, and 7.9 mol of sodium dodecyl sulfate/mol of protein respectively 24, 25, 26, 27, and 28, ovalbumin bound with 0.3, 0.9, 3.1,4.8, and 8.2 mol of linoleate/mol of protein respectively. Interfacial tension measured at corn oil/0.20c protein interface with a Fisher Surface Tensiontat Model 21. Emulsifying activity index calculated from the absorbance at 500 nm of the supernatant after centrifuging blended mixtures of 2 ml of corn oil and 6 ml of 0.5% protein in 0.01 M phosphate buffer, pH 7.4 S initial slope of fluorescence intensity (FI) vs. percent protein plot. 10 /al of 3.6 mM m-parinaric acid solution was added to 2 ml of 0.002 to 0.1% protein in 0.01 M phosphate buffer, pH 7.4, containing 0.002% SDS. FI was measured at 420 nm by exciting at 325 nm. (From Ref. 2. Reprinted by permission.)...

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