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Assay Development for Lysyl Hydroxylase: A new HPLC method for efficient separation of lysine- from hydroxylysine-containing peptides (Paperback)

Deepak Patel

ISBN 10: 3639222571 / ISBN 13: 9783639222579
Editorial: VDM Verlag, Germany, 2010
Nuevos Condición: New Encuadernación de tapa blanda
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Language: English. Brand new Book. Hydroxylysine is produced as a posttranslational modification mainly in collagens, the most abundant protein in mammals. Lysyl hydroxylase (LH) is the enzyme that catalyzes the formation of hydroxylysyl residues in collagen by hydroxylation of -X-Lys-Gly- sequences. In order to study the hydroxylation reaction catalysed by LH, we have synthesized 4 different peptides and the corresponding hydroxylated peptide using Fmoc solid-phase methodology. Peptides have been characterized by HPLC, mass spectrometry and CD spectroscopy. A new HPLC method for efficient separation of lysine- from hydroxylysine-containing peptides has been developed in both organic (1-anthroylnitrile as derivatizating reagent) and aqueous phase (dansyl chloride as derivatizating reagent). Peptides derivatization is done prior to HPLC analysis. The products (di- and tetra-substituted lysine- and hydroxylysine- containing peptides) have been fully separated by HPLC and their structure confirmed by MALDI-TOF MS analysis. Efficient separation of derivatized peptides will allow for the convenient and rapid measurement of LH activity by HPLC methods. N° de ref. de la librería KNV9783639222579

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Detalles bibliográficos

Título: Assay Development for Lysyl Hydroxylase: A ...

Editorial: VDM Verlag, Germany

Año de publicación: 2010

Encuadernación: Paperback

Condición del libro: New

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Hydroxylysine is produced as a posttranslational modification mainly in collagens, the most abundant protein in mammals. Lysyl hydroxylase (LH) is the enzyme that catalyzes the formation of hydroxylysyl residues in collagen by hydroxylation of -X-Lys-Gly- sequences. In order to study the hydroxylation reaction catalysed by LH, we have synthesized 4 different peptides and the corresponding hydroxylated peptide using Fmoc solid-phase methodology. Peptides have been characterized by HPLC, mass spectrometry and CD spectroscopy. A new HPLC method for efficient separation of lysine- from hydroxylysine-containing peptides has been developed in both organic (1-anthroylnitrile as derivatizating reagent) and aqueous phase (dansyl chloride as derivatizating reagent). Peptides derivatization is done prior to HPLC analysis. The products (di- and tetra-substituted lysine- and hydroxylysine- containing peptides) have been fully separated by HPLC and their structure confirmed by MALDI-TOF MS analysis. Efficient separation of derivatized peptides will allow for the convenient and rapid measurement of LH activity by HPLC methods.

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