Abstract: The present invention relates to methods for producing a polypeptide having biological activity, comprising: (a) cultivating a fungal host cell in a medium conducive for the production of the polypeptide, wherein the fungal host cell comprises a first polynucleotide encoding the polypeptide operably linked to a second polynucleotide encoding a variant signal peptide or a variant prepropeptide; and (b) isolating the secreted polypeptide having biological activity from the cultivation medium.

Abstract: Compositions and methods for the treatment of asthma and inflammatory ocular disorders are disclosed.

Abstract: A method of secretory expression of lysostaphin in Escherichia coli at high level, which comprises constructing a expression vector by cloning a sequence encoding a signal peptide which is suitable for secretory expression in Escherichia coli before part or whole gene sequence which encodes mature lysostaphin, and ligating the cloned sequence with a promoter; and transforming Escherichia coli with the expression vector, culturing and fermenting, and then isolating lysostaphin from the supernatant of the fermentation broth. The advantage of secretory expression is that the expression product can exist in the medium in an active form, and thus does not need the process for renaturation of the inclusion body; it is more easily to purify from the supernatant of the fermentation broth with high rate of recovery; and there is less contamination from the host's proteins.

Abstract: The present invention provides an isolated archael and bacterial heme binding protein which reversibly binds oxygen with a low affinity. The heme binding protein may be utilized as a blood substitute. The invention also provides a method for controlled storage of oxygen by contacting a bacterial heme binding protein with oxygen allowing the protein to bind and store oxygen. The also provides methods to sense gaseous ligands using the heme binding protein. In other embodiments, the invention provides chimeric proteins having a heme-binding domain of an isolated heme binding archael bacterial protein and a heterologous signaling domain.

Abstract: The present invention is based on the identification of a series of virulence genes in E. coli K1, the products of which may be implicated in the pathogenicity of the organisms. The identification of the genes allows them, or their expressed products, to be used in a number of ways to treat infection.

Abstract: A universal secretory signal originally derived from a piscine vitellogenin (Vtg) gene is inserted into various expression vectors for driving the secretion of the recombinant protein into the culture medium. This enhances the detection, quantification and downstream scaled-up purification of a recombinant protein of interest. The secretory signal system is very versatile, being conveniently and widely applicable to an array of heterologous host cells such as bacteria, yeast, insect, piscine, and mammalian cell lines (e.g., COS, CHO, NIH/3T3). The said secretory system is also applicable as a reporter vector for secretion of reporter proteins/enzymes, thus, enabling the detection of the reporter proteins (e.g., CAT, GFP) in the culture medium.

Abstract: Oligopeptides which comprise amino acid sequences that are recognized and proteolytically cleaved by free prostate specific antigen (PSA) are described. Also described are assays which comprise such oligopeptides useful for determining free PSA protease activity in vitro and in vivo. Therapeutic agents which comprise conjugates of such oligopeptides and known cytotoxic agents are also described.

Abstract: Phthalyl amidase is an enzyme previously unknown in the art that catalyzes removal of the phthalyl moiety from phthalyl-containing amides. The current invention provides DNA compounds encoding the phthalyl amidase enzyme and methods for expressing such compounds. The present invention also provides recombinant DNA vectors encoding phthalyl amidase and host cells transformed with these DNA vectors.