5399490 Vector to produce biologically important peptides

5399490 Vector to produce biologically important peptides

PATENT ABSTRACTS 5399483 EXPRESSION OF MDR-RELATED GENRE IN YEAST CELL Shibano Yuji; Ueda Kazumitsu; Komano Tohru Osaka, JAPAN Assigned to Suntory Li...

65KB Sizes 2 Downloads 52 Views

PATENT ABSTRACTS

5399483 EXPRESSION OF MDR-RELATED GENRE IN YEAST CELL Shibano Yuji; Ueda Kazumitsu; Komano Tohru Osaka, JAPAN Assigned to Suntory Limited A yeast host which can express P-glycoprotein, i.e., the product of MDR-related gene, in the cell membrane in the same state as observed in multidrug resistant cells produced by connecting the MDR-related gene which carries multidrug resistance to a yeast expression vector and transforming the yeast with said recombinant vector; a cell membrane fraction eontnining a substantial amount of P-glycoprotein produced by said yeast and a process for the preparation thereof; and a recombinant vector for expressing the MDR-related gene in a yeast host.

5399489 PRODUCTION OF PROTEINS IN PROCARYOTES Krivi Gwen G St Louis, MO, UNITED STATES Assigned to Monsanto Company A method for preparing polypeptides in bacteria with an alanine rather than a methionine at the Nterminus. The DNA sequence expressed has an alanine codon immediately following from one to about three contiguous methionine codous including a translation start signal and allows for the expression of polypeptides having the amino acid sequence of, for example, naturally occurring eucaryotic proteins such as various bovine and porcine somatotropin species.

53~4~ VECTOR TO PRODUCE BIOLOGICALLY IMPORTANT PEPTIDES Balganesh Tanjore S; Das Goutam; Visweswariah Sandhya S Bangalore, INDIA Assigned to Aktiebolnget Astra In this patent application we have described the construction of a novel secretion vector based on E. coli enterotoxin coding sequence. We have shown categorically that pre and pro regions of

569

toxin gene are absolutely necessary for extra cellular secretion of the stable toxin. We have also shown with specific examples that when the nucleotide coding sequence of a heterologous peptide is fused in frame to the end of the pro region in the st gene, the resultant vector in an E. coli host secretes extracelhilarly correctly processed heterologous peptide. This application also includes coustruction of suitable vectors where this gene fusion can be achieved. Generally methods to create such fusions involving a) recombinant DNA technology and b) the use of site directed in vitro mutagenesis, have also been described. A general method of purification of heterologous peptides is also described in this application. This novel vector system can be used for hyperproduction and extracelhilar secretion of peptides of biological importance.

5399491 NUCLEIC ACID SEQUENCE AMPLIFICATION METHODS Kacian Daniel L; Fultz Timothy J San Diego, CA, UNITED STATES Assigned to Gen-Probe Incorporated Methods of synthesizing multiple copies of a target nucleic acid sequence autocatalytically under conditions of substantially constant temperature, ionic strength, and pH are provided in which multiple RNA copies of the target sequence autocatalytically generate additional copies. These methods are useful for generating copies of a nucleic acid target sequence for purposes which include assays to quantitate specific nucleic acid sequences in clinical, environmental, forensic and similar samples, cloning and generating probes.

~9~93 METHODS AND COMPOSITIONS FOR THE OPTIMIZATION OF H U M A N HEMATOPOIETIC PROGENITOR CELL CULTURES Emerson Stephen G; Clarke Michael F; Palsson Bernhard; Schwartz Richard Ann Arbor, MI, UNITED STATES Assigned to The Regents of the University of Michigan Methods, including culture media conditions, which provide for ex vivo human stem cell