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Biotech / Medical : XOMA. Bull or Bear? -- Ignore unavailable to you. Want to Upgrade?

To: Robert K. who wrote (12229)	11/15/1999 8:12:00 AM
From: ballydog1	Respond to of 17367

If I were the FDA.... hmmmm. Yes, I admit to being a skeptic even if I'm not the FDA. Don't want anyone else telling me what to think. Not ever. Nevertheless, I might have an intelligent question or two if the party providing the information wasn't too pushy or insistent. I might even want to be walked through the results, to make it easier for me to make a decision. Its use it or lose it. French DNA hunting dogs (not poodles!) just happen to be my breed of preference here, although I am a dog lover. Witness my participation on this board. Standard Ballydog1 disclaimer applies

To: Robert K. who wrote (12229)	11/16/1999 10:11:00 AM
From: aknahow	Respond to of 17367

Robert, Nov. 9 patent. Ellsbach not XOMA?? Or does XOMA have rights to it?? The BPI fragments of the present invention are as potent as the holoprotein against rough E. coli, more potent than the holoprotein against the generally more resistant, smooth E. coli (on a molar basis), and retain the specificity of the holoprotein towards gram-negative bacteria. This is a particularly important finding because smooth gram-negative bacteria (smoothness being due to the presence of longer LPS chains in the bacterial cell membrane) generally are more pathogenic than their corresponding rough counterparts. Patent number 5,980,897 Due to its potent bactericidal action against gram-negative bacteria and lack of cytotoxicity towards other microorganisms and eukaryotic cells, it is envisioned that BPI may be employed as a chemotherapeutic agent and/or as a model for the design of new antibiotic agents. However, due to its large molecular weight (58 kDa for the human holoprotein), both sequencing and determination of the structural organization of BPI have been hampered (hereinafter the entire BPI molecule is referred to as the holoprotein). The possibility has been raised that, as in the case with other cytotoxic proteins, BPI as a structural organization where the different functions, namely binding, envelope-altering and killing reside in different domains within the BPI molecule. Although BPI fragments, obtained by digestion of the holoproteins with the proteolytic enzyme elastase, has been disclosed (Weiss, J. et al., Clin. Res 34: 537A, 1986), the fragments tested remained associated under the non-denaturing conditions employed. No biological activity was ascribed to any isolated fragments. Moreover, antibodies directed against the holoprotein did not recognize these fragments under denaturing conditions when analyzed using the well-known Western blotting procedure. Therefore, in light of the above, there is a need in the art for biologically active peptide fragments of BPI for use as bactericidal/permeability increasing agents as well as therapeutic agents. Such fragments are also needed to provide sequence information on BPI to direct the design of future generations of antimicrobial agents specific for gram-negative bacteria and to be used as probes into the molecular organization of the holoproteins.