Application of high performance liquid chromatography combined with diode‐array detection for analysis of proteins and peptides in human cerebrospinal fluid

Silberring, Jerzy; Nyberg, Fred; Lyrenäs, Sven

doi:10.1002/bmc.1130030506

Cited by 9 publications

(3 citation statements)

References 13 publications

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“…Ventricular CSF was collected from patients suffering from increased intracerebral pressure and selected for shunt surgery [26]. Purification was performed with material obtained from individual patients.…”

Section: Methodsmentioning

confidence: 99%

Identification of bikunin as an endogenous inhibitor of dynorphin convertase in human cerebrospinal fluid

et al. 2006

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Dynorphin-converting enzymes (DCEs) constitute a recently identified group of proteinases capable of transforming the dynorphin-related opioid peptides to enkephalins [1,2]. The total activity of these enzymes in the central nervous system is surprisingly high compared to the peptide pool in tissues or body fluids [3]. These enzymes convert the j-receptor-specific dynorphins to d-receptor-specific enkephalins, and may play an important role by releasing ligands mediating analgesic activity [4,5]. One of these enzymes is a serine peptidase that has shown to be present in human [6] and rat [7] cerebrospinal fluid (CSF). Little is known about the regulation of the activity of neuropeptide peptidases in the central nervous system. Recently, we described our preliminary finding of a protein in the CSF [2] possessing inhibitory activity against a DCE isolated from CSF. Here, we present a detailed study on the identification and properties of this inhibitor, which also inhibited other serine proteases such as trypsin, chymotrypsin and plasmin. Results Isolation of inhibitorWe had earlier isolated a DCE in the CSF that was found to be a serine protease. Therefore, to isolate and identify an endogenous inhibitor of this enzyme, we used affinity chromatography with an immobilized anhydrotrypsin. In the case of bikunin from human

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Section: Methodsmentioning

confidence: 99%

Identification of bikunin as an endogenous inhibitor of dynorphin convertase in human cerebrospinal fluid

et al. 2006

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“…HPSEC, combined with multispectral detection by a photodiode-array (PDA) UV detector was applied to the analysis of proteins and peptides in human cerebrospinal fluid (CSF) [125] and to the characterization of proteinergic profiles in the CSF of alcoholics [ 126]. Molecular components of the CSF were identified, and their purity was tested.…”

Section: Detectorsmentioning

confidence: 99%

Chapter 5 Size-exclusion chromatography

Silberring¹,

Kowalczuk²,

Bergquist³

et al. 2004

Journal of Chromatography Library

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“…In certain cases derivatization of amino acids allowed the monitoring of changes in the UV/VIS absorption spectra during the chemical reaction (Lundblad and Noyes, 1984b), which served as evidence of the progress of the reaction. The multispectral analysis was also successfully applied to direct identification of single aromatic amino acids (Fell et ul., 1984;Nozaki, 1990); interfacing of photodiode array detectors to the high performance liquid chromatographic (HPLC) instruments extended the investigations to the analysis of aromatic residues in peptides and their metabolites (Nyberg et ul., 1986) or in proteins present in the body fluids (Silberring et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Application of photodiode array detection and fast atom bombardment mass spectrometry for the identification of the arginine residue in neuropeptides

Silberring

Nyberg

1991

Biomedical Chromatography

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Chemical derivatization by phenylglyoxal (PGX) was applied to the identification of arginine in the neuropeptides dynorphin A (1-6) and substance P. The obtained products were separated on a short reversed phase C18 column and analysed on-line with the photodiode array UV technique. The selective attachment of a chromogenic molecule into the arginine residue resulted in significant change in the absorbance spectra around 250 nm, depending on the number of PGX molecules attracted. Further analysis employed fast atom bombardment mass spectrometry (FAB MS) and C-terminal sequencing for detailed verification of the derivatives formed during modification with PGX. The results clearly demonstrated that the photodiode array technique, when combined with chemical modification of certain amino acids, provides new possibilities for the analysis of peptide structures.

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Application of high performance liquid chromatography combined with diode‐array detection for analysis of proteins and peptides in human cerebrospinal fluid

Cited by 9 publications

References 13 publications

Identification of bikunin as an endogenous inhibitor of dynorphin convertase in human cerebrospinal fluid

Identification of bikunin as an endogenous inhibitor of dynorphin convertase in human cerebrospinal fluid

Chapter 5 Size-exclusion chromatography

Application of photodiode array detection and fast atom bombardment mass spectrometry for the identification of the arginine residue in neuropeptides

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