Abstract: Provided is a tire puncture sealant having improved puncture sealing performance while showing excellent storage stability. The present invention relates to a tire puncture sealant including: rubber latex, a tackifying resin emulsion, and a rosin acid surfactant.

Abstract: A method for producing a protein suitable for X-ray crystallographic analysis, in a cell-free protein synthesis system comprising a cell-free extract, a nucleic acid coding for said protein, and amino acids for the substrate of said protein, wherein said amino acids comprises at least one amino acid comprising a heavy atom, and wherein the introduced rate of said amino acid comprising the heavy atom into the synthesized protein is at least 80%.

Abstract: Light-colored phenolic-modified rosin esters, suitable for use as, for example, tackifiers in adhesive compositions, are prepared by reacting together rosin, a phenolic compound, formaldehyde or a reactive equivalent thereof, and a non-phenolic hydroxyl-containing organic compound in the presence of at least one lightening agent selected from phenol sulfide compounds, phosphorous acid, esters of phosphorous acid, and hypophosphite salts. The formaldehyde or reactive equivalent is present in an amount ranging from about 1.1 to about 3.5 equivalents of --CHO moieties per 1 equivalent of Ar--OH moiety of the phenolic compound, in order to obtain rosin esters having desirably low color, and adequately low molecular weight to effectively function as tackifiers.

Abstract: Rosin esters that are both light colored and color stable are produced by reacting polyhydric alcohol with an equivalent excess of rosin, in the presence of calcium bis(monoethyl(3,5-di-tert-butyl-4-hydroxybenzyl)phosphonate. When phosphinic acid is added to the reaction mixture, light colored and color stable rosin esters are produced regardless of whether the rosin or polyol are in equivalent excess, although preferably the rosin is in equivalent excess. It is preferred to include a phenol sulfide compound, such as Vultac.RTM. 2, with the calcium bis(monoethyl(3,5-di-tert-butyl-4-hydroxybenzyl)phosphonate, and to add the phosphinic acid incrementally after the acid number of the rosin and polyhydric alcohol reaction mixture has dropped to about 100. Excess rosin is preferably stripped from the product mixture at about 275.degree. C.

Abstract: An improved, stable rosin ester tackifier consisting essentially of an adduct of rosin and a polyhydric alcohol selected from the group consisting of trimethylolpropane, trimethylolethane, and mixtures thereof, and hot melt adhesive compositions consisting essentially of said tackifier and a polymer component, said compositions containing a mixture of antioxidants containing a higher alkyl diester of thiopropionic acid, a hindered phenolic compound and a phenol sulfide compound, preferably an alkyl phenol disulfide oligomer.

Abstract: The catalytic combination of a phosphite ester and a phenol sulfide is disclosed. The catalyst combination accelerates and mediates the esterification reaction of rosin with a polyhydric alcohol, resulting in esterified rosins having numerous advantageous characteristics and particular utility as tackifiers in hot melt adhesives.

Abstract: This invention relates to a method for treating polymerized rosin to decrease its tendency to oxidize comprising heating the polymerized rosin to an elevated temperature in the presence of an effective amount of one or more disproportionating agents. This invention also relates to the novel products of such disproportionation treatments.

Abstract: The color stability of rosin esters is improved by carrying out the esterification reaction in the presence of 0.05% to 5% sodium hydroxymethane sulfonate (SHS). The color stability of polymerized rosin is improved by heating at a temperature of 250.degree.-290.degree. C. in the presence of SHS.

Abstract: A novel 92-kDa type IV collagenase has been purified to homogeneity from SV-40 transformed fetal lung fibroblasts, its primary structure determined and characterized and a cDNA clone representing the full size protein has been developed.