Proteins against

Hepatitis B Hepatitis B vaccines provide another illustration of how drug products have advanced vdth increasing technical capability. Vaccination against hepatitis B is common pradice for health workers, travellers and others who may be at risk of exposure to the virus. The initial vaccines contained inactivated virus to promote the immune response necessary to proted against future infection by the live virus. However, there was always some concern in case there was not complete inactivation of the virus used for vaccination. Further research into the virus identified the surface proteins against which the immune response is raised. The genetic... 

Schuster, G., Even, D., Kloppstech, K. Ohad, I. (1988). Evidence for protection by heat-shock proteins against photoinhibition during heat-shock. EMBO Journal, 7, 1-6. 

A step closer toward realism is taken by off-lattice models in which the backbone is specified in some detail, while side chains, if they are represented at all, are taken to be single, unified spheres [44-50]. One indication that this approach is too simplistic was given in [51], which proved that for a backbone representation in which only Ca carbons were modeled, no contact potential could stabilize the native conformation of a single protein against its nonnative ( decoy ) conformations. However, Irback and co-workers were able to fold real protein sequences, albeit short ones, using a detailed backbone representation, with coarse-grained side chains modeled as spheres [49, 52-54]. 

Although acquired immunity to some parasitic diseases may lower the level of infection, absolute immunity as seen in bacterial and viral infections is seldom seen in parasitic diseases. Since parasitic infections produce a wide variety of antigens because of the many life cycle phases, it is more difficult to identify a constant antigenic protein against which specific antibodies are protective. However, malaria remains a likely candidate for a vaccine and there are ongoing studies to develop one. 

Stabilization of proteins against those degradative processes with retention of structure and function through removal of water requires an understanding of the process of lyophilization or freeze-drying. 

In summary, formalin-treated does not significantly perturb the native structure of RNase A at room temperature. It also serves to stabilize the protein against the denaturing effects of heating as revealed by the increase in the denaturation temperature of the protein. However, formalin-treatment does not stabilize RNase A sufficiently to prevent the thermal denaturation of the protein at temperatures used in heat-induced AR methods as shown by both DSC and CD spectropolarimetry. This denaturation likely arrises from the heat-induced reversal of formaldehyde cross-links and adducts, as shown in Figure 15.4 of Section 15.4. Further, cooling formalin-treated RNase A that had been heated to 95°C for 10 min does not result in the restoration of the native structure of the protein, particularly in regard to protein tertiary structure. 

Sah H (1999) Stabilization of proteins against methylene chloride/water interface induced denaturation and aggregation. J Control Release 58 143-151... 

According to X-ray and neutron diffraction structures [3, 4] the binding of CO to the heme leads to a bent FeCO unit. The Fe-C-O angle is, however, found to be linear in synthetic models of the protein (hiomimetic molecules). Because of this, it was originally thought that the FeCO distortion was responsible for the well known discrimination of the protein against CO - the affinity ratio C0/02 is lower in the protein than in biomimetic systems [1]. In... 

Interfacial interaction between silicone and protein/starch microparticle, 3 and the use of polysiloxanes having hydrophilic groups for the stabilization of proteins against denaturation, 4 were studied. 

Hipkiss, A. R. and Chana, H. (1998). Carnosine protects proteins against methylglyoxal-mediated modifications. Biochem. Biophys. Res. Commun. 248, 28-32. 

Calculation of the molecular mass of an unknown protein follows the same procedure as, for example, quantitative protein determination plotting of the Rf of the calibration proteins against their molecular mass computing of a standard curve and estimation of the MW of the unknown protein and using the regression functions of the standard curve (c.f Fig. 2.1). 

Methods were described for the incorporation of proteins in the form of noncovalent complexes with polycationic reagents, into sustained release systems where the polycation stabilizes the protein against inactivation while it resides in the delivery device, and retards release of the protein from the delivery device [469,470]. A variety of polycations have been used, including simple polyamino acids such as polylysine or polyarginine, protamine and chitosan. The end result was the release of the active agent with retention of biological activity, with a high cumulative field and over a sustained period of time. 

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