Abstract: DNA sequences from potato which encode the enzyme solanidine UDP-glucose glucosyltransferase (SGT) are disclosed. Recombinant DNA molecules containing the sequences, and use thereof, in particular, use of an antisense DNA construct to inhibit the production of SGT and thereby reduce glycoalkaloid levels in solanaceous plants, e.g., potato, are described.

Abstract: A hybridoma cell lines is described which produces and secretes a monoclonal antibody which selectively binds to the glycoalkaloids of potatoes, tomatoes, and eggplants, as well as their corresponding aglycones. Glycoalkaloids of potatoes, tomatoes, and/or eggplants in biological samples may be detected and quantified by contacting the sample with the antibodies to form a glycoalkaloid/antibody immunocomplex when the glycoalkaloids are present, which immunocomplex may then be detected. The monoclonal antibody may also be incorporated into kits for the detection and quantification of glycoalkaloids in plants, foods, and body tissues and fluids.

Abstract: Hybrid cell lines (hybridomas) which produce and secrete high affinity monoclonal antibodies specific for Bowman-Birk inhibitor (BBI) are described. High affinity antibodies to BBI are described that have one or more of the following additional characteristics: (1) they are specific to the active form of BBI, that is, they react and bind with undenatured BBI, but do not bind with BBI which has been denatured by heat or disulfide exchange; (2) they do not react and bind with KTI; (3) they distinguish classical BBI from other BBI's including lima bean protease inhibitor; and (4) they bind BBI-protease complex, e.g., BBI-chymotrypsin. Immunoassay methods using the monoclonal antibodies to analyze BBI specifically in plant, animal or human tissue or fluid or foodstuffs and techniques for immunoaffinity binding of BBI are described.

Abstract: Hybrid cell lines (hybridomas) which produce and secrete high affinity monoclonal antibodies specific for Bowman-Birk inhibitor (BBI) are described. High affinity antibodies to BBI are described that have one or more of the following additional characteristics: (1) they are specific to the active form of BBI, that is, they react and bind with undenatured BBI, but do not bind with BBI which has been denatured by heat or disulfide exchange; (2) they do not react and bind with KTI; (3) they distinguish classical BBI from other BBI's including lima bean protease inhibitor; and (4) they bind BBI-protease complex, e.g., BBI-chymotrypsin. Immunoassay methods using the monoclonal antibodies to analyze BBI specifically in plant, animal or human tissue or fluid or foodstuffs and techniques for immunoaffinity binding of BBI are described.

Abstract: Hybrid cell lines (hybridomas) which produce and secrete monoclonal antibodies with three distinct patterns of recognition are described. The first specificity pattern is defined by antibodies which (1) recognize Kunitz trypsin inhibitor (KTI), one of the principal protease inhibitors found in soybeans, but do not detect the Bowman-Birk inhibitors (BBI), the other major class of protease inhibitors in soybeans; (2) bind to native KTI isoforms a and b but do not react with KTI isoforms a and b which have been denatured by moist heat or alkaline treatment or which have been subjected to disulfide exchange; and (3) do not recognize native KTI isoform c.

Abstract: Proteinaceous fibers are modified by first contacting the fibers with an aqueous solution of a cupric salt of a carboxylic acid containing from 2-18 carbon atoms and then contacting the so-treated fibers with a hot, semipolar, water-miscible organic solvent. The modified fibers exhibit increased resistance to shrinkage.

Abstract: Lysinoalanine formation during alkaline treatment of edible proteinaceous material containing lysine is inhibited by acetylating the .epsilon.-amino group of the lysine prior to treatment of the material with alkali. Both lysinoalanine and lanthionine formation are inhibited in the alkaline treatment of keratinous fibers containing lysine by acylating the .epsilon.-amino group of lysine with an acyl moiety containing from one to eight carbon atoms.

Abstract: Proteinaceous feed material is contacted with certain compounds to render it more suitable for ruminant animals. The so-treated proteinaceous material is resistant to degradation in the rumen of the animals but is readily degraded and digested in the intestines thereof.

Abstract: Method for inhibiting the formation of lysinoalanine when proteinous material is treated by alkali, which comprises conducting the alkali treatment in the presence of a compound selected from the group consisting of sulfhydryl-containing amino acids, their esters, and amides.

Abstract: Wool is flameproofed and shrinkproofed by a process wherein the wool is reacted simultaneously with a halogenated acid anhydride and an isocyanate in the presence of cresol. The flameproofing treatment is durable to both aqueous laundering and drycleaning.

Abstract: Wool is modified by reacting it with a wool-modifying reagent (e.g., tetrabromophthalic anhydride) in the presence of a reaction promoter (e.g., dimethylformamide) and a low-boiling inert solvent (e.g., dichloromethane), at an ambient temperature of about 100.degree. to 120.degree. C., and in an open vessel to permit evaporation of the low-boiling solvent.

Abstract: The flame resistance of wool is enhanced by treating it with chlorendic acid. The treatment is carried out in a manner similar to conventional dyeing, or in conjunction with dyeing. Typically, the wool is contacted with a hot aqueous medium containing chlorendic acid and a dye.