Antigen stability

HBeAg reagent, positive genetically engineered HBe antigen, stabilized with bovine serum albumin and Synperonic, lyophilised, preservative phenol (max. 1 g/L)... 

It is possible to achieve this rapid purification only by careful attention to the preparation and properties of the immunoadsorbent used to extract the specific antibody molecules. Immunoadsorbents can be prepared in a very wide variety of ways. The criteria to be satisfied in the choice of an immunoadsorbent are as follows a chemically inert solid phase high capacity for binding antigen stability of the antigen-solid phase bond low nonspecific uptake by the immunoadsorbent of protein other than antibody and a high antibody-binding capacity. 

Venkatachalam, M., Tenber, S.S., Peterson, W.R., Roux, K.H., and Sathe, S.K., Antigenic stability of pecan [Carya illinoinensis (Wangenh.) K. Koch] proteins Effects of thermal treatments and in vitro digestion, J. Agric. Food Chem., 54, 1449-1458, 2006. 

The mast cell stabilizers currently for ophthalmic use are nedocromil and pemirolast. These drugp are used for the prevention of eye itching caused by allergic conjunctivitis. The mast cell stabilizers act by inhibiting the antigen-induced release of inflammatory mediators (eg, histamine) from human mast cells. 

In vivo reproducible results can only be achieved if the liposome-drug or -antigen combinations are thoroughly characterized upon preparation in terms of their physical and chemical properties and, besides, if the stability during storage is ensured. In this chapter both the pharmaceutical (preparation, characterization, and stability) aspects and the therapeutic potentials and limitations of drug and antigen delivery with liposomes will be discussed. 

Antibody A52 with its epitope at residues 657-672 [129,139,274,275] inhibited the vanadate-induced crystallization of Ca " -ATPase and decreased the stability of preformed Ca " -ATPase crystals [285]. The vanadate-induced crystals arise by the association of the ATPase monomers into dimers (type A interaction), the dimers into dimer chains (type B interaction), and the dimer chains into 2-dimensional arrays (type C interaction). It is suggested that antibody A52 interferes with type B interactions, preventing the formation of dimer chains, without exerting major effect on the concentration of Ca -ATPase dimers in the membrane. The simplest interpretation of the destabilization of Ca -ATPase crystals by mAb A52 is that binding of the antibody to its antigenic site physically blocks the interaction between ATPase molecules [285]. Considering the large bulk of the antibody, such interference is not unexpected, yet only a few of the antibodies that bind to the Ca -ATPase in native sarcoplasmic reticulum interfered with crystallization. 

The human caliciviruses, norovirus (NoV) and sapovirus, have also been described as small round structured viruses, for their 27-30 nm capsids. The NoV capsid consists of 180 copies of the VPl major capsid protein packed as an icosahedron (Prasad et ah, 1999) and the VP2 minor capsid protein, which may contribute to stability (Bertolotti-Ciarlet et al., 2002). The S domain of VPl forms the inner shell of the capsid, while the P domain protrudes from the capsid surface and contributes to binding the histoblood group antigen receptor (Cao et ah, 2007) and antigenicity (Donaldson et ah, 2008 Lindesmith et ah, 2010). 

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