Abstract: The present invention relates to the gene for stilbene synthase, isolated from plants, and its use for the transformation of vectors, host organisms and plants, as well as to the production of plants which have an increased resistance to pests.

Abstract: A method of testing for target bacteria involves adding bacteriophage to a sample to infect the bacteria in the sample; killing extracellular bacteriophage without at the same time killing phage-infected bacteria; amplifying bacteriophage remaining in the sample; and causing the bacteriophage to infect reporter bacteria and thereby produce an observable signal. The reporter bacteria are genetically engineered to have an indicator gene which on expression gives rise to a detectable signal, wherein expression of the indicator gene is initiated on bacteriophage infection of the bacteria.

Abstract: Disclosed is a novel protein which has a molecular weight of 45,000.+-.5,000 and pI 5.7.+-.0.5 and exhibits cancer metastasis-inhibitory activity. The protein can be prepared by culturing human cells, animal cells and microorganisms capable of producing the protein in a nutrient culture medium while stimulating them with an inducer such as Bacille Calmette-Guerin and lipopolysaccharide.

Abstract: DNA molecules encoding a modified tryptophan synthase beta subunit are disclosed. When expressed in a recombinant host microorganism, these polypeptide analogs enable significant levels of intracellular indole production and accumulation. In the presence of an aromatic dioxygenase enzyme, the indole so produced can be converted to indoxyl, which upon exposure to air oxidizes to indigo.

Abstract: This invention provides a cell comprising a DNA molecule having a regulatory element from a gene, other than a gene encoding a green-fluorescent protein operatively linked to a DNA sequence encoding the green-fluorescent protein. This invention also provides a method for selecting cells expressing a protein of interest which comprises: a. introducing into the cells a DNAI molecule having DNA sequence encoding the protein of interest and DNAII molecule having DNA sequence encoding a green-fluorescent protein; b. culturing the introduced cells in conditions permitting expression of the green-fluorescent protein and the protein of interest; and c. selecting the cultured cells which express green-fluorescent protein, thereby selecting cells expressing the protein of interest. Finally, this invention provides various uses of a green-fluorescent protein.

Abstract: Disclosed herein are purified isolated mammals polypeptides having the property of potentiating the bacterial growth inhibitory activity of bactericidal/permeability-increasing protein and pharmaceutical formulations comprising these polypeptides. Also disclosed is a method for obtaining mammalian polypeptides having the property of potentiating the bacterial growth inhibitory activity of bactericidal/permeability-increasing protein potentiating activity, and methods for treating gram-negative bacterial infections in mammals and for neutralizing lipopolysaccharides. Also disclosed is a method for the treatment of diseases caused by endotoxins in mammals.

Abstract: A process for the in vitro production of chemically modified polyphenolic polymer (PPP). First, stable, highly active extracellular tyrosinase is produced from genetically transformed microorganism such as Streptomyces antibioticus. The tyrosinase is then incubated with a reaction substrate such as 1-tyrosine, hydrolyzed protein, or an oligopeptide in combination with 1-tyrosine. The ratio of the oligopeptide/tyrosine combination as well as variation in the concentration of tyrosinase can be used to modify the color, the molecular size, and the spectral absorbance properties of the PPP produced. Alternatively, or additionally, oxidants such as hydrogen peroxide or hypochlorite can be used to modify the color of the PPP, regardless of the method used to produce the PPP, and the PPP can subsequently be fractionated using molecular weight cut-off ultrafiltration. Organic solvents can also be used in the method of making PPP to produce PPPs having variable but reproducible physical properties.

Abstract: The DNA encoding glucan synthesis gene 1 (GLS1) is cloned and used in an in vitro assay to screen for compounds that modulate 1,3.beta.-D glucan synthase activity.

Abstract: A modified maxadilan protein exhibits higher biological activity than native maxadilan from the sand fly Lutzomyia longipalpis. A modified maxadilan fusion protein contains a thrombin cleavage site. This enables the production of the modified maxadilan as a fusion protein and recovery of the modified maxadilan after digestion with thrombin. The modified maxadilan is a potent vasodilator.

Abstract: Single-chain analogs of the naturally occurring two-chain peptide monellin retain the sweetening properties of the natural protein and are stable under conditions which would otherwise destabilize the native peptide. A covalent linkage joins peptides corresponding to portions of the A and B chains of the naturally occurring protein.

Abstract: Methods are disclosed for producing thrombin. The protein is produced from host cells transformed or transfected with DNA construct(s) containing information necessary to direct the expression of thrombin precursors. The DNA constructs generally include the following operably linked elements: a transcriptional promoter, DNA sequence encoding a gla-domainless prothrombin, and a transcriptional terminator. Thrombin precursors produced from transformed or transfected host cells are activated either in vivo or in vitro.

Abstract: The present invention provides the isolated genes encoding marine melA from the genus Shewanella, especially from the species S. colwelliana, and the melA encoded thereby in homogeneous form. Further, the invention provides antibodies to marine melA as well as methods of using the melA to induce oyster larval settlement. Moreover, these marine melA genes are also useful as selectable markers for genetic engineering.

Abstract: DNA encoding a novel human .beta..sub.2 integrin .alpha. subunit polypeptide, designated .alpha..sub.d, is disclosed along with methods and materials for production of the same by recombinant procedures. Binding molecules specific for .alpha..sub.d are also disclosed as useful for modulating the biological activities of .alpha..sub.d. DNA from other species which show homology to human .alpha..sub.d encoding sequences are also disclosed.

Abstract: Substantially pure enterotoxins of Shigella flexneri 2a are described, along with a method for obtaining the same, antibodies having binding specificity to the enterotoxins and a method for use of the enterotoxins to develop a non-reactogenic Shigella flexneri 2a vaccine candidate.

Abstract: The present invention succeeds in isolating a gene encoding an enzyme having an FMN reducing activity and a nitroreductase activity derived from luminous bacteria Vibrio fischeri (ATCC 7744), elucidating its primary structure, and producing Escherichia coli which can express the gene in large quantities. That is, the present invention provides a gene encoding an enzyme having the flavin reducing activity and the nitro-reductase activity, an enzyme produced therefrom, a recombinant vector containing the gene, and bacteria containing the recombinant vector.

Abstract: A process for the in vitro production of chemically modified polyphenolic polymer (PPP). First, stable, highly active extracellular tyrosinase is produced from genetically transformed microorganism such as Streptomyces antibioticus. The tyrosinase is then incubated with a reaction substrate such as l-tyrosine, hydrolyzed protein, or an oligopeptide in combination with l-tyrosine. The ratio of the oligopeptide/tyrosine combination as well as variation in the concentration of tyrosinase can be used to modify the color, the molecular size, and the spectral absorbance properties of the PPP produced. Alternatively, or additionally, oxidants such as hydrogen peroxide or hypochlorite can be used to modify the color of the PPP, regardless of the method used to produce the PPP, and the PPP can subsequently be fractionated using molecular weight cut-off ultrafiltration. Organic solvents can also be used in the method of making PPP to produce PPPs having variable but reproducible physical properties.

Abstract: A substantially pure non-glycosylated human interleukin-2 protein having a specific activity of not less than 10.sup.4 U/mg is obtained by growing a transformant carrying a DNA having a base sequence coding for human interleukin-2 to cause production and accumulation of human interleukin-2 in the culture broth, subjecting the thus obtained human interleukin-2-containing liquid to a purification process comprising a hydrophobic column chromatography.

Abstract: This invention allows high-purity maltose to be manufactured both simply and economically by sequentially going through the steps of liquefaction of starch, saccharification of the resulting liquefied substance by combining with general-purpose enzymes and further saccharification with an enzyme which hydrolyzes oligosaccharides of trisaccharide or more, and also allows the economical and favorable manufacturing of maltitol, the reduced product of the above maltose, by going through an additional reduction step.

Abstract: The subject invention concerns novel peptides which have the property of interfering with the biosynthesis of the enzyme trypsin and the biosynthesis of the hormone ecdysone. This property enables the use of these peptides to, for example, inhibit the formation of progeny in blood-ingesting insects, e.g., Neobellieria, since trypsin is an essential enzyme for food digestion which provides the essential building blocks for egg development in such insects.

Abstract: A microorganism belonging to the genus Pseudomonas; an alkaline lipase produced by the microorganism or its mutants; a method of producing the alkaline lipase; and detergents containing the alkaline lipase as an aid, the alkaline lipase having (1) an operative pH of from 4 to 11.5, and an optimum pH of from 7.0 to 9.5, as measured using triolein emulsion as a substrate; (2) an operative temperature of from 10.degree. to 80.degree. C., and an optimum temperature of from 55.degree. to 65.degree. C., as measured using triolein emulsion as a substrate; (3) a molecular weight of 28,000 .+-.2,000 as measured by electrophoresis using SDS polyacrylamide; (4) isoelectric point of 4.5 .+-.1.5 as measured by isoelectric focusing polyacrylamide gel electrophoresis; and (5) an inhibition of lipase activity by a detergent component of not higher than 50% as measured using sodium linear-alkylbenzenesulfonate as said detergent component.