CAS: 52946-88-0; Pyridin-2-Ylglycine

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上下游产品

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📜(吡啶-2-基氨基)-乙腈置于盐酸体系中,化学反应生成 N-2-吡啶基甘氨酸
参考文献:275.有机化合物的颜色.第八部分 异构体染料从3的比较:7一-Diazaindan-1-酮和-2-酮
标题:275.有机化合物的颜色.第八部分 异构体染料从3的比较:7一-Diazaindan-1-酮和-2-酮
摘要:
DOI:10.1039/jr9560001360

专利信息

专利号:EP-0528854-B1
优先权日:1990-04-17
标题 :Fluorogenic peptides and their use in the determination of enzymatic activities
发明人：MELDAL MORTEN; BREDDAM KLAUS
权利人:CARLSBERG AS
摘要:A fluorogenic peptide exhibiting intramolecular quenching having the general formula F-A-Q-Y1 or Y2-Q-A-F wherein Q is a fluorescence quenching substituted amino acid residue (I) wherein R1, R2, R3, R4 and R5 are independently selected from hydrogen, hydroxy, alkyl, alkoxy, amino, nitro, amido, halogen, aryl or aralkyl, with the proviso that at least one of R1 to R5 is hydroxy and at least one is nitro, wherein X is a spacing group which may be absent or selected from any combination of -CO-NH-, -CO-O-, -S-, -S-S-, -O-, -NH- or -C6H4-, and n and m are integers from 0 to 10, F is a fluorescent group having a maximum emission within the absorption band for the quenching residue Q, A is a spacing entity selected from amino acid residues and peptide residues and may include a non-peptide molecular entity, e.g. a mono- or oligosaccharie being linked to the fluorescent group F via an amide bond or ester bond, Y1 is OH, NH2, an amino acid residue, a peptide residue which is preferably attachable to a solid phase or a C-terminal protective group, Y2 is H, an amino acid residue, a peptide residue or an N-terminal protective group. Preferred peptides are those, wherein Q is 3-nitro-tyrosine, i.e. F1-A1-Tyr(NO2)-Y1 wherein F1 is a fluorescent group having a maximum emission of from 400 to 460 nm, preferably anthraniloyl, A1 is an amino acid residue or a peptide residue, preferably having 2 to 15 amino acids, and linked to the group F via a peptide bond, and Y1 is as defined above. The peptides are useful as substrates for determination of enzymatic activities in a sample, e.g. biological systems by incubating with the sample under conditions favourable to enzymatic activities, and determining and comparing the fluorescence emitted before and after the incubation. The peptides may advantageously be prepared by parallel multi-column solid phase synthesis.