Abstract: A process for preparing difucosyl Y.sub.2 antigen (dimeric Le.sup.x) , said process comprising: (1) preparing a lactonorhexaosylceramide backbone or a lactonorhexaosylsaccharide backbone linked to a carrier molecule; and (2) enzymatically fucosylating said backbone at the III.sup.3 and V.sup.3 positions through an .alpha.1.fwdarw.3 linkage. A process for preparing Le.sup.y antigen analogues, said process comprising: (1) preparing a lactonorhexaosyl-ceramide backbone or a lactonorhexaosylsaccharide backbone linked to a carrier molecule; and (2) enzymatically fucosylating said backbone at the terminal .beta.-Gal through an .alpha.1.fwdarw.2 linkage; and (3) enzymatically fucosylating said backbone at one or more positions through an .alpha.1.fwdarw.3 linkage, provided that steps (2) and (3) can be conducted simultaneously or in any order.

Abstract: The present invention relates to Bacillus polymyxa Haitai 1 (KCCM-10001) capable of producing polysaccharides which are viscous and thermally stable, and have the capacities of water holding, film forming and emulsifying, and can reversibly form a gel when heated, and to polysaccharides having the above characteristics which are produced by utilizing the said microorganism.

Abstract: Fermentation product A83543, comprising major components A83543A and A83543D and minor components A83543B, A83543C, A83543E, A983543F, A83543G, A83543H and A83543J, is produced by a newly described species, Saccharopolyspora spinosa. The A83543 components and their acid-addition salts (A83543 compounds) are useful as insecticides, particularly against Lepidoptera and Diptera species. Insecticidal, miticidal or ecto-parasiticidal combinations, compositions and methods are provided.

Abstract: A transparent and stable aqueous solution of a substrate for a determination of lipase, comprising triglyceride uniformly solubilized therein, a method for determination of lipase activity in a sample, employing the aqueous solution, and a process for the manufacture of a lyophilized product capable of forming the aqueous solution are disclosed. A process for the manufacture of a transparent and stable aqueous solution of triglyceride is also disclosed.

Abstract: Esters or amides of a peptide, preferably a dipeptide, consisting essentially of natural or synthetic L-amino acids with hydrophobic side chains were found to have specific cellular toxicities. Preferable amino acids of the peptide are leucine, phenylalanine valine, isoleucine, alanine, proline, glycine or aspartic acid beta methyl ester. Preferable dipeptides are L leucyl L-leucine, L-leucyl L-phenylalanine, L-valyl L-phenylalanine, L-leucyl L-isoleucine, L-phenylalanyl L-phenylalanine, L-valyl L-leucine, L-leucyl L-alanine, L-valyl L-valine, L-phenylalanyl L leucine, L prolyl L-leucine, L-leucyl L-valine, L-phenylalanyl L-valine, L glycyl L-leucine, L-leucyl L-glycine, glycyl L-phenylalanine and L-aspartyl beta methyl ester L-phenylalanine. Most preferable dipeptides are L-leucyl L-leucine, L-leucyl L-phenylalanine, L-valyl L-phenylalanine, L-phenylalanyl L-leucine, L-leucyl L-isoleucine L-phenylalanyl L-phenylalanine and L-valyl L-leucine.

Abstract: P. elodea mutants are produced which produce gellan gum broth which contains no detectable amount of poly-.beta.-hydroxy-butyrate (PHB).

Abstract: The present invention provides a process for preparing ganglioside G.sub.Ml characterized in that neuraminidase isozyme S is allowed to act on gangliosides to produce ganglioside G.sub.Ml.

Abstract: Described is a process for producing an immunosuppressant, "demethimmunomycin" (L-683,7411) a C-31 demethylated analog of L-683,590 under fermentation conditions utilizing the microorganism, Actinoplanacete sp, (Merck Culture Collection MA 6559) ATCC No. 53771. The macrolide immunosuppressant is useful in preventing human host rejection of foreign organ transplants, e.g. bone marrow and heart transplants.

Abstract: The invention describes diagnostic methods and compositions for determining the amount of protease in a body fluid sample. In particular, the invention detects proteases by a method in which both a reversible inhibitor of the protease and an irreversible inhibitor of interfering proteases during the detection step are employed to increase the sensitivity of the enzyme capture assay. The assay detects normal serum levels of activated protein C.

Abstract: A galactomannan heteropolysaccharide is prepared by fermentation of a previously unknown microorganism, named Erwinia sp. ATCC No. 55046. The polysaccharide has valuable properties as a thickening, suspending, stabilizing and lubricating agent in aqueous systems. It has a chemical composition of mannose, galactose and galacturonic acid in the approximate molar ratio of 5:3:2. The polysaccharide can be produced in high yield and volumetric productivity from a submerged culture fermentation of a low-cost, lactose-containing whey or whey permeate medium.

Abstract: A process for the continuous conversion of cephalosporin derivatives into glutaryl-7-aminocephalosporanic acid derivativesA process for the continuous conversion of cephalosporin derivatives into the corresponding glutaryl-7-aminocephalosporanic acid derivatives in the presence of a catalyst containing D-amino-acid oxidase is described. The product yield can be increased, where appropriate, by addition of hydrogen peroxide.

Abstract: The present invention is directed to a process for purifying and characterizing "myotrophin", a novel soluble protein factor that is believed to regulate myocardial hypertrophy in hypertension. In addition, the invention is directed to the purified and partially characterized protein factor produced by the process of the present invention, as well as uses of this factor, or its antagonist to control cardiac hypertrophy.

Abstract: The invention provides improved methods for assaying samples for the presence of a beetle luciferase. The methods of the invention entail improved kinetics of light production from luciferase activity in beetle luciferase-luciferin reactions.

Abstract: This invention provides a pullulanase having a high degree of pH stability under acidic conditions, which is produced by cultivation of a microorganism belonging to the genus Bacillus, particularly Bacillus circulans SV-98 (FERM P-12161). This enzyme is useful, for example, in the manufacture of glucose and maltose from starch.

Abstract: The aspartame content in aqueous solutions is determined by enzymatic cleavage of aspartame to aspartic acid and phenylalanine methyl ester by means of a peptidase, followed by a detection reaction cocatalyzed by adenine dinucleotide. The phenylalanine is, after elimination of the ester group by means of chymotrypsin, converted by phenylalanine dehydrogenase in the presence of NAD.sup.+ into phenylpyruvate, and the aspartame concentration is measured via the NADH or NH.sub.3 formation which occurs as a consequence. Alternatively, the aspartic acid is converted by a cell extract which acts on aspartic acid in the presence of NADP.sup.+, and the resultant NADPH or NH.sub.3 is used to determine aspartame concentration. These enzymatic reactions preferably are carried out in consecutive enzyme columns with carrier-immobilized enzymes by the FIA technique. The proportion of hydrolysis products can be measured by analyzing another sample omitting the peptidase reaction.

Abstract: Benanomicin A and Benanomicin B are fermentatively produced by the cultivation of a new microorganism Actinomadura spadix, designated as MH193-16F4 strain.

Abstract: An aqueous coenzyme reagent composition contains NADH, a carbonate/bicarbonate buffer (with a pH of about 9.5-11) and water. Both NADH and the buffer are at low concentrations, e.g., about 2-5 mM for NADH and about 2-15 mM for carbonate/bicarbonate. When this coenzyme reagent is mixed with an enzyme reagent, the mixture achieves a neutral pH. The combination of high pH, low NADH concentration and low buffer concentration permit the aqueous reagent to be stored for extended periods at low temperatures without NADH degrading to form impurities which interfere with or inhibit enzyme activity, such as the activity of lactate dehydrogenase or malate dehydrogenase in an assay for ALT or AST.

Abstract: The invention relates to methods and means for quantitative determination of the isoaspartyl content of polypeptides via selective methylation of their fragments, catalyzed by a protein L-isoaspartyl methyltransferase enzyme. Since deamidation of asparagine side chains at specific sites of proteins and the resultant isoaspartate formation are emerging as a major contributor to protein degradation under mild conditions, the invention also concerns a method for quantitation of protein degradation associated with isoaspartate formation.

Abstract: This invention relates to methods for producing optically active hydroxyesters and also to methods for producing and purifying optically active five-membered ring lactones.More specifically, the invention provides methods for efficiently, safely, and selectively producing and purifying optically active (R)-hydroxyester (shown by formula 1) and optically active (S)-hydroxyester (shown by formula 2) in high state of purity at ordinary temperature.The invention also relates to application of the interconvertible optically active (R)-five-membered ring lacton (shown by formula 5).They are intermediates for synthesizing various medicines, agricultural chemicals, and biologically active substances, however especially useful for synthesizing pheromone of a noxious insect, Popillia japonica Newman. ##STR1## (Here, R.sub.1 denotes --C.tbd.C--R.sub.3 or --C.dbd.C--R.sub.3 ; R.sub.2 and R.sub.3 denote straight chain or branched alkyl groups containing 1 to 10 carbon atoms; R.sub.

Abstract: A dry analytical element for the determination of serum cholinesterase (CHE) activity is disclosed. The element analyses undiluted body fluids and employs butyrylthiocholine as the substrate for CHE. Butyrylthiocholine is hydrolyzed by serum cholinesterase and liberates butyric acid and thiocholine. The thiocholine liberated then reduces ferricyanide to ferrocyanide and the rate of change is measured by reflectance densitometry.