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Results for “Diethyl Pyrocarbonate”

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At least 109 records · Page 6Linked to original sources
PubMed1992

Inactivation of a beta-glucosidase from Arthrobotrys conoides by diethyl pyrocarbonate: evidence of histidine at the active site.

Modification of A. conoides beta-glucosidase by diethylpyrocarbonate caused rapid inactivation of the enzyme. The kinetic analyses showed that the inactivation by diethylpyrocarbonate resulted from the modification of an average of one histidine residue per mole of enzyme. The modified enzyme showed an increase in absorbance at 240 nm. Sulphydryl, lysine and tyrosine residues were not modified by diethylpyrocarbonate treatment. The substrate offered significant protection against diethylpyrocarbonates modification. The results indicate that diethylpyrocarbonate was interacting with the enzyme at or near the active site.

Binding Sites↗
PubMed1992

Chemical modification of glucosamine-6-phosphate synthase by diethyl pyrocarbonate: evidence of histidine requirement for enzymatic activity.

Glucosamine-6-phosphate synthase from Escherichia coli was inactivated by diethylpyrocarbonate at pH 7.3 and 4 degrees C with a second-order rate constant of 1220 M-1 min-1. The difference spectrum of inactivated vs native enzyme had a maximum absorption at 242 nm, which is characteristic of N-carbethoxyhistidine. No trough at around 280 nm due to O-carbethoxytyrosine was observed and the sulfhydryl content of the enzyme was unchanged. Studies with [14C]diethylpyrocarbonate provided evidence that derivatization of a single histidine residue of the amino-terminal glutamine-binding domain inactivated glucosamine-6P synthase. These results are consistent with the participation of an histidine residue in a catalytic triad, Cys/His/Asp, necessary to generate ammonia from glutamine.

Binding Sites↗
PubMed1990

Stabilization of tumor antigens by chemical modification with diethyl pyrocarbonate.

C3H mice were immunized with MH134 tumors modified with two different chemicals, DEPC and TNBS, and the tumor-neutralizing activities of the spleen cells were examined after separating the cells by a Nylon-wool column, plastic dish, or treatment with specific antibodies (anti-mouse IgG and anti-mouse theta sera). The effector cells induced in mice by immunization with TNBS-treated tumors were T cells. In contrast, in the case of tumors modified with DEPC, macrophages were the major effector cells. The effects of chemical modification on the solubilization of cell surface proteins was also examined. DEPC inhibited solubilization of specific proteins from tumor cell surfaces, while TNBS did not have such an effect on the solubilization of proteins. These results indicate that the antitumor response in mice primed with DEPC-modified tumor is different from the case of TNBS-modified tumors, and that the immunological significance of chemical modification with DEPC is supposedly due to the stabilization of antigenic proteins on the tumor cell surface.

Animals↗