Lysozyme continued

Continuous free flow electrophoresis has been used for the separation of biopolymers (e.g. ovalbumin and lysozyme) [20] as well as smaller inorganic species (e.g. [Co sepulchrate)] and [Co (CN)g] ) [21]. Sample processing rates of 15 mg h were reported for a mixture of Amaranth (MW 804) and Patent Blue VF (MW 1159) [22]. 

The kinetics of disulfide formation, the demonstration of specific binding, and the immunochemical results all support the conclusion that native-like structure results from the oxidative folding of reduced peptide 13-105. These three independent lines of evidence support the conclusion that lysozyme has a continuous chain independent assembly region somewhere in the sequence 13-105. 

Similarly, Chow et al. observed an increase in the lysozyme activity of a soluble lung fraction and of plasma after continuous exposure of rats to ozone at 0.8 ppm for 8 days. However, no difference in lung or plasma lysozyme activity from control values was present in rats continuously exposed to 0.2 or 0.5 ppm or intermittently exposed (0.2-0.8 ppm, 8 h/day for 7 days). Histochemical evidence of an increase in lung acid phosphatase, a lysosomal enzyme, has also been reported. ... 

Continuous for 8 days Increased activity of lung and plasma lysozyme (no effect at 0.2 and 0.5 ppm) Rat 31... 

Using a cylindrical internal reflectance (CIRcle) cell and GC-IR data collection software, it was determined for both lysozyme and BPN, that most of the enzyme adsorption occurred within ten seconds after injection. Nearly an order-of-magnitude more BPN adsorbed on the hydrophobic surface than the hydrophilic one, while lysozyme adsorbed somewhat more strongly to the hydrophilic Ge surface. Over time periods of about one day, the lysozyme layer continued to increase somewhat in thickness, while BPN maintained its initial coverage. 

Figure 15.2. Results of energy minimization with SPDBV. The minimization results (per residues) of turkey lysozyme (UEF.pdb) are shown in two frames (upper frame and continuing lower frame).

Fig. 10. Comparison of sequences of a-lactalbumins and lysozymes, including a key to the abbreviations. The highest numbers of residues showing homology in a given position are boxed with continuous lines, the next highest are boxed in broken lines, and the third highest are boxed in dotted lines, a-la, a-Lactalbumin Iz, lysozyme. For further details see text. (Reproduced from H. A. McKenzie. Copyright 1983—1989 by H. A. McKenzie.)...

Jolles and Joll s (1984) have reviewed the use of lysozyme as a marker in certain diseases. Serum lysozyme levels have been used extensively in the diagnosis of leukemias. Jolles and Jolles discussed some of the reasons for increased and decreased serum levels in various diseases, such as acute or chronic granulocytic leukemia, myeloid metaplasia, and aplastic anemia, and decreased levels in tears in keratoconjunctivitis. They have also considered the interaction of lysozyme with sulfated proteoglycans and its role in the calcification of epiphyseal cartilage. It is to be expected that such studies will yield valuable information, giving rise to further applications in the future (see also Fett et al., 1985). Lysozyme will continue, of course, to serve as a prototype protein for the investigation of the specificity of immune recognition. 

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