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NEW FLUORESCENT PROBE WHICH IS OBTAINED BY MODIFYING BOTH ENDS OF SUBSTRATE PEPTIDE WITH FLUORESCENT LIGHT- EMITTING COMPOUNDS AND IS USED FOR DETECTING ACTIVITY OF CASPASE
NEW FLUORESCENT PROBE WHICH IS OBTAINED BY MODIFYING BOTH ENDS OF SUBSTRATE PEPTIDE WITH FLUORESCENT LIGHT- EMITTING COMPOUNDS AND IS USED FOR DETECTING ACTIVITY OF CASPASE
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机译:通过用荧光发光化合物修饰底物肽的两端而获得的新的荧光探针,用于检测Caspase的活性
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摘要
PROBLEM TO BE SOLVED: To obtain a new fluorescent probe which is obtained by modifying both the ends of a substrate peptide capable of being specifically cleaved with caspase with a combination of fluorescent light-emitting compound residues that the fluorescent light spectrum of one fluorescent light group is overlapped on the fluorescent light spectrum of the other fluorescent light group, and enables the observation in the change of fluorescent light with the passage of time. ;SOLUTION: A new fluorescent light probe of the formula: fluorescent light group D-amino acid sequence-fluorescent group A (the fluorescent light group D and the fluorescent group A are a combination of fluorescent light-emitting compound residues wherein the fluorescent light spectrum of one fluorescent light group capable of being excited with visible light is overlapped on the fluorescent light spectrum of the other fluorescent light group capable of being excited with visible light; the amino acid sequence is a ≤100 Å long amino acid sequence) is obtained by modifying both the ends of a substrate peptide having an amino acid sequence capable of being specifically cleaved with caspase with a combination of the fluorescent light-emitting compound residues wherein the fluorescent light spectrum of one fluorescent light group capable of being excited with visible light is overlapped on the fluorescent light spectrum of the other fluorescent light group capable of being excited with visible light. The activity of the caspase in a cell can quantitatively be observed by the change in the specific fluorescent light ratio of the fluorescent light groups bound to both the ends of the substrate peptide chain capable of being specifically cleaved with the caspase with the passage of time.;COPYRIGHT: (C)2000,JPO
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