Research ExplorerPublicationsMass-spectrometry-linked screening of protein fractions for ...

Mass-spectrometry-linked screening of protein fractions for enzymatic activities--a tool for functional genomics

Standard

Mass-spectrometry-linked screening of protein fractions for enzymatic activities--a tool for functional genomics. / Jankowski, J; Stephan, N; Knobloch, M; Fischer, S; Schmaltz, D; Zidek, W; Schlüter, H.

In: ANAL BIOCHEM, Vol. 290, No. 2, 03.2001, p. 324-9.

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

Harvard

Jankowski, J, Stephan, N, Knobloch, M, Fischer, S, Schmaltz, D, Zidek, W & Schlüter, H 2001, 'Mass-spectrometry-linked screening of protein fractions for enzymatic activities--a tool for functional genomics', ANAL BIOCHEM, vol. 290, no. 2, pp. 324-9. https://doi.org/10.1006/abio.2001.5001

APA

Jankowski, J., Stephan, N., Knobloch, M., Fischer, S., Schmaltz, D., Zidek, W., & Schlüter, H. (2001). Mass-spectrometry-linked screening of protein fractions for enzymatic activities--a tool for functional genomics. ANAL BIOCHEM, 290(2), 324-9. https://doi.org/10.1006/abio.2001.5001

Vancouver

Jankowski J, Stephan N, Knobloch M, Fischer S, Schmaltz D, Zidek W et al. Mass-spectrometry-linked screening of protein fractions for enzymatic activities--a tool for functional genomics. ANAL BIOCHEM. 2001 Mar;290(2):324-9. https://doi.org/10.1006/abio.2001.5001

Bibtex

@article{c950ae3dc9084836b398789bdea704ac,
title = "Mass-spectrometry-linked screening of protein fractions for enzymatic activities--a tool for functional genomics",
abstract = "A simple and rapid strategy is described to screen protein fractions for defined enzymatic activity. A protein fraction from a porcine kidney extract was immobilized by covalent coupling to activated affinity beads. The immobilized proteins were incubated with probes specific for different enzyme activities. The reaction products were analyzed by matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry. The MALDI spectra indicate the presence of 5'-nucleotidase, phosphatase, kinase, glutathione reductase, and renin activities in the kidney protein extract. Furthermore, the method can be used to screen for inhibitors of enzymatic reactions. The method is adaptable to high-throughput sample handling and automated mass spectrometric analysis and therefore suited for functional genomics.",
keywords = "Animals, Electrophoresis, Polyacrylamide Gel, Enzyme Inhibitors, Enzymes, Kidney, Microspheres, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Substrate Specificity, Swine, Time Factors, Journal Article, Research Support, Non-U.S. Gov't",
author = "J Jankowski and N Stephan and M Knobloch and S Fischer and D Schmaltz and W Zidek and H Schl{\"u}ter",
note = "Copyright 2001 Academic Press.",
year = "2001",
month = mar,
doi = "10.1006/abio.2001.5001",
language = "English",
volume = "290",
pages = "324--9",
journal = "ANAL BIOCHEM",
issn = "0003-2697",
publisher = "Academic Press Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - Mass-spectrometry-linked screening of protein fractions for enzymatic activities--a tool for functional genomics

AU - Jankowski, J

AU - Stephan, N

AU - Knobloch, M

AU - Fischer, S

AU - Schmaltz, D

AU - Zidek, W

AU - Schlüter, H

N1 - Copyright 2001 Academic Press.

PY - 2001/3

Y1 - 2001/3

N2 - A simple and rapid strategy is described to screen protein fractions for defined enzymatic activity. A protein fraction from a porcine kidney extract was immobilized by covalent coupling to activated affinity beads. The immobilized proteins were incubated with probes specific for different enzyme activities. The reaction products were analyzed by matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry. The MALDI spectra indicate the presence of 5'-nucleotidase, phosphatase, kinase, glutathione reductase, and renin activities in the kidney protein extract. Furthermore, the method can be used to screen for inhibitors of enzymatic reactions. The method is adaptable to high-throughput sample handling and automated mass spectrometric analysis and therefore suited for functional genomics.

AB - A simple and rapid strategy is described to screen protein fractions for defined enzymatic activity. A protein fraction from a porcine kidney extract was immobilized by covalent coupling to activated affinity beads. The immobilized proteins were incubated with probes specific for different enzyme activities. The reaction products were analyzed by matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry. The MALDI spectra indicate the presence of 5'-nucleotidase, phosphatase, kinase, glutathione reductase, and renin activities in the kidney protein extract. Furthermore, the method can be used to screen for inhibitors of enzymatic reactions. The method is adaptable to high-throughput sample handling and automated mass spectrometric analysis and therefore suited for functional genomics.

KW - Animals

KW - Electrophoresis, Polyacrylamide Gel

KW - Enzyme Inhibitors

KW - Enzymes

KW - Kidney

KW - Microspheres

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

KW - Substrate Specificity

KW - Swine

KW - Time Factors

KW - Journal Article

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

U2 - 10.1006/abio.2001.5001

DO - 10.1006/abio.2001.5001

M3 - SCORING: Journal article

C2 - 11237335

VL - 290

SP - 324

EP - 329

JO - ANAL BIOCHEM

JF - ANAL BIOCHEM

SN - 0003-2697

IS - 2

ER -