Activity and fluorescent derivatives of aminotyrosyl trypsin and trypsinogen

Neurath, Hans; Kenner, R. A.

doi:10.1021/bi00780a002

Cited by 34 publications

(1 citation statement)

References 17 publications

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“…Although much less reactive than aliphatic amines at neutral pH, the aromatic amine of o-aminotyrosine can selectively react with amine-reactive reagents at lower pH. 491,492 Namely, Nikov et al 492 have demonstrated that selective labelling of aminotyrosines is achievable in the presence N-terminal and e-amino groups of lysines by using NHS-activated ester at particular reaction conditions (acetate buffer, pH 5.0, 2 hours). Exploitation of the pK a difference between aminotyrosyl residues and other reactive groups in proteins (4.75 for aminotyrosine, whilst much higher values for N-terminal and side-chain amino groups, see Section 1.1) allows selective labelling thereof.…”

Section: Tyrosinementioning

confidence: 99%

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

2015

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Bioconjugation methodologies have proven to play a central enabling role in the recent development of biotherapeutics and chemical biology approaches. Recent endeavours in these fields shed light on unprecedented chemical challenges to attain bioselectivity, biocompatibility, and biostability required by modern applications. In this review the current developments in various techniques of selective bond forming reactions of proteins and peptides were highlighted. The utility of each endogenous amino acid-selective conjugation methodology in the fields of biology and protein science has been surveyed with emphasis on the most relevant among reported transformations; selectivity and practical use have been discussed.

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Section: Tyrosinementioning

confidence: 99%

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

2015

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Organische Fluoreszenzreagentien für die Untersuchung von Enzymen und Proteinen

Kanaoka

1977

Angewandte Chemie

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Organic Fluorescence Reagents in the Study of Enzymes and Proteins

Kanaoka

1977

Angew. Chem. Int. Ed. Engl.

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Studies designed to elucidate life processes require close cooperation between various scientific disciplines. A pertinent example is seen in the application of fluorescence spectroscopy to biological studies, where biological sciences, physical and organic chemistry, and technical innovations complement one another. This report reviews the application of fluorescence probes which bind covalently to certain sites of proteins. The major organic fluorescence reagents used in this field are tabulated.

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Activity and fluorescent derivatives of aminotyrosyl trypsin and trypsinogen

Cited by 34 publications

References 17 publications

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation

Organische Fluoreszenzreagentien für die Untersuchung von Enzymen und Proteinen

Organic Fluorescence Reagents in the Study of Enzymes and Proteins

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