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

To: Jinping Shi who wrote (8107)	12/22/1998 10:07:00 AM
From: aknahow	Respond to of 17367

Good to see your post. Of course I don't agree. The directors continue living in the U.S. or wherever they live or want to live. The operations continue in the U.S. as the prospectus clearly states. I also think the vote will be close. Too bad! The issue seems clear and as I have posted before, once one removes the change of domicile issue from the subject of XOMA, it becomes clear that this idea is a good one for biotech companies with the potential to generate foreign revenue. The issue for XOMA will be decided on the 29th. However, I still believe we will see change of domicile proposals from others in 1999. It will be interesting to follow the reactions. In many cases I believe they will be less emotional.

To: Jinping Shi who wrote (8107)	12/23/1998 12:36:00 PM
From: aknahow	Read Replies (1) \| Respond to of 17367

Any views on patent 5851802? Claims follow below: Claims 1. A recombinant DNA vector construct suitable for introduction into a bacterial host comprising a coding sequence for a fusion protein having: (a) at least one cationic bactericidal/permeability-increasing (BPI) peptide encoding DNA sequence; (b) a carrier protein encoding DNA sequence; and (c) an amino acid cleavage site encoding DNA sequence located between the sequences (a) and (b), wherein the construct additionally encodes a bacterial secretory leader sequence at the amino-terminus of the fusion protein and wherein the encoded BPI peptide has anti-bacterial activity. 2. The vector construct of claim 1, wherein the coding sequence for the fusion protein is 5'-(b)-(c)-(a)-3'. 3. The vector construct of claim 1, wherein the anti-bacterial encoded BPI peptide also has anti-fungal activity. 4. The vector construct of claim 1, wherein the anti-bacterial encoded BPI peptide also has endotoxin-binding activity. 5. The vector construct of claim 1, wherein the anti-bacterial encoded BPI peptide also has heparin-binding activity. 6. The vector construct of claim 1, wherein the encoded carrier protein is a cationic carrier protein. 7. The vector construct of claim 1, wherein cationic carrier protein is selected from the group of gelonin and the D subunit of human osteogenic protein. 8. The vector construct of claim 1, wherein the encoded BPI peptide has an amino acid sequence given in any one of the sequences SEQ ID NOS. 1-239. 9. The vector construct of claim 1, wherein the encoded amino acid cleavage site is selected from the group of codons encoding Asp-Pro, Met, Trp and Glu. 10. A bacterial host cell transformed with the vector construct of claim 1. 11. An E. coli host cell according to claim 10. 12. A method for bacterial production of a cationic BPI peptide comprising the steps of: (a) culturing a transformed bacterial host cell according to claim 10 under conditions allowing expression therein of the fusion protein; (b) isolating the expressed fusion protein; (c) cleaving the expressed fusion protein to release the cationic BPI peptide; and (d) isolating the cationic BPI peptide. 13. A method for bacterial production of a cationic BPI peptide comprising the steps of: (a) culturing a transformed bacterial host cell according to claim 10 under conditions allowing expression therein of the fusion protein; (b) cleaving the expressed fusion protein to release the cationic BPI peptide; and (c) isolating the cationic BPI peptide. 14. A method for bacterial production of a fusion protein comprising the steps of: (a) culturing a transformed bacterial host cell according to claim 10 under conditions allowing expression therein of the fusion protein; and (b) isolating the expressed fusion protein. 15. The fusion protein product of the process of claim 14.