Bio-technology General Corporation

American Cyanamid Company

Meir Fischer

Avigdor Levanon

Moshe M Werber

Elisha P Zeelon

Deborah Tardy Chaleff

Rachel Guy

Amos Panet

Meir Rigbi

Daniel Bartfeld

Benjamin Greenman

Michael R Lebens

Ruth Lifshitz

Arie Goldlust

Plasmids are provided which upon introduction into a suitable Eschericia coli host render the host capable of effecting expression of DNA encoding a desired naturally-occurring polypeptide or polypeptide analog thereof under the control of the deo P1-P2 promoter. Further plasmids are also provided which thermoinducibly direct expression of eucaryotic genes under the control of a .lambda. P.sub.L promoter and a thermolabile repressor protein present on the same plasmid under the control of a deo P1 promoter. These plasmids have been inserted into various hosts, some of which contain DNA encoding the repressor protein. Such plasmids may be used to produce polypeptides such as human copper/zinc superoxide dismutase, hMnSOD-hGPX fusion polypeptides, human manganese superoxide dismutase, human growth hormone, bovine growth, porcine growth, human growth hormone-apolipoprotein E fused polypeptides, apolipoprotein E and various fibronectin domains.

Expressions plasmids containing the deo promoter, and bacterial hosts

Plasmids are provided which upon introduction into a suitable host render the host capable of effecting expression of DNA encoding a desired polypeptide under the control of an osmB promoter. Such plasmids may be used to produce polypeptides such as superoxide dismutases, acetylcholinesterase, growth hormones and hepatitis antigen.

Expression plasmids regulated by an osmB promoter

The present invention provides a recombinant polypeptide having the amino acid sequence X-tyr.sup.26 -gly.sup.110 where tyr.sup.26 -gly.sup.110 is identical to the sequence shown in FIG. 10, and wherein X is methionine or absent and wherein asn.sup.72 may be substituted by pro. The invention further provides a method of producing the polypeptide which comprises transforming a host cell with an expression plasmid encoding the polypeptide, culturing the transformed host cell so that the cell produces the polypeptide encoded by the plasmid, and a method of recovering the polypeptide so produced.

Production of recombinant factor Xa inhibitor of leech Hirudo

Expression plasmids regulated by an OSMB promoter

Plasmids are provided which upon introduction into a suitable Escherichia coli host render the host capable of effecting expression of DNA encoding a desired naturally-occurring polypeptide or polypeptide analog thereof under the control of the deo P1-P2 promoter. Further plasmids are also provided which thermoinducibly direct expression of eucaryotic genes under the control of a .lambda. P.sub.L promoter and a thermolabile repressor protein present on the same plasmid under the control of a deo P1 promoter. These plasmids have been inserted into various hosts, some of which contain DNA encoding the repressor protein. Such plasmids may be used to produce polypeptides such as human copper/zinc superoxide dismutase, hMnSOD-hGPX fusion polypeptides, human manganese superoxide dismutase, human growth hormone, bovine growth, porcine growth, human growth hormone-apolipoprotein E fused polypeptides, apolipoprotein E and various fibronectin domains.

Expression plasmids containing the deo promoter, and bacterial hosts

The present invention relates to somatotropin analogues with amino acid changes in the alpha-helix 1 regions of said somatotropins, alone or in combination with mutations in the alpha-helix 3 and/or alpha-helix 2 regions, plus combinations with other changes to the native amino acid sequence of somatotropins. The resulting analogues are stable for formulation in sustained release formulations, while maintaining biological activity. Further, methods for conducting site-directed mutagenesis on DNA encoding proteins and/or polypeptide also are provided.

Somatotropins with alterations in the alpha-helix 1 region, and

Applicants describe methods for purifying human ApoE or analog thereof from recombinant bacterial cells with minimal protein aggregation and degradation during the purification process. The invention involves the addition of neutralized fatty acids to the medium during cell disruption and the use of a non-ionic detergent during the purification process. Additionally applicants describe a method for increasing the production of ApoE or analog thereof in a bacterial host by adding to the culture medium neutralized fatty acids, fatty acid precursors, triglycerides, triglyceride precursors or acetate. Pharmaceutical and diagnostic uses of the ApoE analog are described.

Method for production and purification or recombinant Apolipoprotein E

The subject invention provides an enzymatically active nonglycosylated, recombinant, human acetylcholinesterase comprising at least one polypeptide characterized by an amino acid sequence which is substantially identical to the amino acid sequence of naturally-occurring human acetylcholinesterase. The subject invention additionally provides an enzymatically active recombinant human acetylcholinesterase comprising at least one polypeptide characterized by an amino acid sequence in which serine is substituted for cys 611 in the sequence of naturally-occurring, human acetylcholinesterase and an enzymatically active recombinant human acetylcholinesterase comprising at least one polypeptide characterized by the presence of a methionine of the N-terminus of the amino acid sequence of naturally-occurring human acetylcholinesterase.

Growing community of inventors

Rehovot, Israel

Meir Fischer