Research ExplorerPublicationsApplication of cross-flow filtration to the purification of ...

Application of cross-flow filtration to the purification of biologically active peptides in human plasma after incubation with a protease-rich extract

Standard

Application of cross-flow filtration to the purification of biologically active peptides in human plasma after incubation with a protease-rich extract. / Schlüter, H; Krivoy, N; Hürster, A; Ingendoh, A; Karas, M; Zidek, W.

In: J CHROMATOGR A, Vol. 625, No. 1, 13.11.1992, p. 3-11.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Schlüter, H, Krivoy, N, Hürster, A, Ingendoh, A, Karas, M & Zidek, W 1992, 'Application of cross-flow filtration to the purification of biologically active peptides in human plasma after incubation with a protease-rich extract', J CHROMATOGR A, vol. 625, no. 1, pp. 3-11.

APA

Schlüter, H., Krivoy, N., Hürster, A., Ingendoh, A., Karas, M., & Zidek, W. (1992). Application of cross-flow filtration to the purification of biologically active peptides in human plasma after incubation with a protease-rich extract. J CHROMATOGR A, 625(1), 3-11.

Vancouver

Schlüter H, Krivoy N, Hürster A, Ingendoh A, Karas M, Zidek W. Application of cross-flow filtration to the purification of biologically active peptides in human plasma after incubation with a protease-rich extract. J CHROMATOGR A. 1992 Nov 13;625(1):3-11.

Bibtex

@article{6227a7cbbc484e8e8c8e0cd868354a45,
title = "Application of cross-flow filtration to the purification of biologically active peptides in human plasma after incubation with a protease-rich extract",
abstract = "The aim of this study was to find an experimental procedure to purify biologically active peptides from a complex biological matrix (plasma), which was incubated with a protease-rich extract (submandibular gland extract). Special interest was focused on the practicability of cross-flow filtration for this purpose. Therefore, peptides in the incubation mixture were purified with a combination of high-performance liquid chromatographic steps. Purification of biologically active peptides was monitored by a sensitive bioassay and by laser desorption/ionization mass spectrometry. This permitted not only purity control at each purification step but also identification of one of the peptides with vasoconstrictor properties as angiotensin II. This result demonstrates the practicability of cross-flow filtration for extracting enzymatic reaction products from complex substrate-enzyme mixtures during the incubation.",
keywords = "Animals, Electrophoresis, Polyacrylamide Gel, Endopeptidases, Filtration, Humans, Hydrolysis, Male, Peptides, Rats, Rats, Wistar, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Journal Article, Research Support, Non-U.S. Gov't",
author = "H Schl{\"u}ter and N Krivoy and A H{\"u}rster and A Ingendoh and M Karas and W Zidek",
year = "1992",
month = nov,
day = "13",
language = "English",
volume = "625",
pages = "3--11",
journal = "J CHROMATOGR A",
issn = "0021-9673",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Application of cross-flow filtration to the purification of biologically active peptides in human plasma after incubation with a protease-rich extract

AU - Schlüter, H

AU - Krivoy, N

AU - Hürster, A

AU - Ingendoh, A

AU - Karas, M

AU - Zidek, W

PY - 1992/11/13

Y1 - 1992/11/13

N2 - The aim of this study was to find an experimental procedure to purify biologically active peptides from a complex biological matrix (plasma), which was incubated with a protease-rich extract (submandibular gland extract). Special interest was focused on the practicability of cross-flow filtration for this purpose. Therefore, peptides in the incubation mixture were purified with a combination of high-performance liquid chromatographic steps. Purification of biologically active peptides was monitored by a sensitive bioassay and by laser desorption/ionization mass spectrometry. This permitted not only purity control at each purification step but also identification of one of the peptides with vasoconstrictor properties as angiotensin II. This result demonstrates the practicability of cross-flow filtration for extracting enzymatic reaction products from complex substrate-enzyme mixtures during the incubation.

AB - The aim of this study was to find an experimental procedure to purify biologically active peptides from a complex biological matrix (plasma), which was incubated with a protease-rich extract (submandibular gland extract). Special interest was focused on the practicability of cross-flow filtration for this purpose. Therefore, peptides in the incubation mixture were purified with a combination of high-performance liquid chromatographic steps. Purification of biologically active peptides was monitored by a sensitive bioassay and by laser desorption/ionization mass spectrometry. This permitted not only purity control at each purification step but also identification of one of the peptides with vasoconstrictor properties as angiotensin II. This result demonstrates the practicability of cross-flow filtration for extracting enzymatic reaction products from complex substrate-enzyme mixtures during the incubation.

KW - Animals

KW - Electrophoresis, Polyacrylamide Gel

KW - Endopeptidases

KW - Filtration

KW - Humans

KW - Hydrolysis

KW - Male

KW - Peptides

KW - Rats

KW - Rats, Wistar

KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

M3 - SCORING: Journal article

C2 - 12126106

VL - 625

SP - 3

EP - 11

JO - J CHROMATOGR A

JF - J CHROMATOGR A

SN - 0021-9673

IS - 1

ER -