| D008623 |
Mercaptoethanol |
A water-soluble thiol derived from hydrogen sulfide and ethanol. It is used as a reducing agent for disulfide bonds and to protect sulfhydryl groups from oxidation. |
2-ME,2-Mercaptoethanol,2 Mercaptoethanol |
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| D010397 |
Penicillanic Acid |
A building block of penicillin, devoid of significant antibacterial activity. (From Merck Index, 11th ed) |
Acid, Penicillanic |
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| D010446 |
Peptide Fragments |
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. |
Peptide Fragment,Fragment, Peptide,Fragments, Peptide |
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| D002852 |
Chromatography, Ion Exchange |
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins. |
Chromatography, Ion-Exchange,Ion-Exchange Chromatography,Chromatographies, Ion Exchange,Chromatographies, Ion-Exchange,Ion Exchange Chromatographies,Ion Exchange Chromatography,Ion-Exchange Chromatographies |
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| D004228 |
Dithionitrobenzoic Acid |
A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate. |
5,5'-Dithiobis(2-nitrobenzoic Acid),DTNB,Ellman's Reagent,5,5'-Dithiobis(nitrobenzoate),Acid, Dithionitrobenzoic,Ellman Reagent,Ellmans Reagent,Reagent, Ellman's |
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| D000595 |
Amino Acid Sequence |
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. |
Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein |
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| D001618 |
beta-Lactamases |
Enzymes found in many bacteria which catalyze the hydrolysis of the amide bond in the beta-lactam ring. Well known antibiotics destroyed by these enzymes are penicillins and cephalosporins. |
beta-Lactamase,beta Lactamase,beta Lactamases |
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| D001665 |
Binding Sites |
The parts of a macromolecule that directly participate in its specific combination with another molecule. |
Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining |
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| D013056 |
Spectrophotometry, Ultraviolet |
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) |
Ultraviolet Spectrophotometry |
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| D013302 |
Streptomyces |
A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value. |
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