Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation

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Standard

Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation. / Buchardt, O; Elsner, H.; Nielsen, Peter E.; Petersen, L C; Suenson, E.

I: Analytical Biochemistry, Bind 158, Nr. 1, 10.1986, s. 87-92.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Buchardt, O, Elsner, H, Nielsen, PE, Petersen, LC & Suenson, E 1986, 'Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation', Analytical Biochemistry, bind 158, nr. 1, s. 87-92. https://doi.org/10.1016/0003-2697(86)90593-2

APA

Buchardt, O., Elsner, H., Nielsen, P. E., Petersen, L. C., & Suenson, E. (1986). Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation. Analytical Biochemistry, 158(1), 87-92. https://doi.org/10.1016/0003-2697(86)90593-2

Vancouver

Buchardt O, Elsner H, Nielsen PE, Petersen LC, Suenson E. Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation. Analytical Biochemistry. 1986 okt.;158(1):87-92. https://doi.org/10.1016/0003-2697(86)90593-2

Author

Buchardt, O ; Elsner, H. ; Nielsen, Peter E. ; Petersen, L C ; Suenson, E. / Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation. I: Analytical Biochemistry. 1986 ; Bind 158, Nr. 1. s. 87-92.

Bibtex

@article{8d8c188b135b46aeabe4e398b2e091bb,
title = "Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation",
abstract = "A homobifunctional cleavable crosslinking reagent containing a selenoethylene group in the linker, and related reagents, have been synthesized and tested in a model system involving formation of a complex between albumin and cytochrome c. Functionally, complex formation was suggested by albumin inhibition of the ascorbate reduction of cytochrome c. Structurally, complex formation was demonstrated by crosslinking and subsequent separation of crosslinked complex from non-crosslinked proteins by SDS-polyacrylamide gel electrophoresis. The crosslinks were found to be cleavable by mild oxidation with low concentrations of periodate or with N-chlorobenzenesulfonamide immobilized on polystyrene beads (Iodo-Beads).",
keywords = "Albumins, Cross-Linking Reagents, Cytochrome c Group, Oxidation-Reduction, Protein Binding, Proteins, Selenium",
author = "O Buchardt and H. Elsner and Nielsen, {Peter E.} and Petersen, {L C} and E. Suenson",
year = "1986",
month = oct,
doi = "10.1016/0003-2697(86)90593-2",
language = "English",
volume = "158",
pages = "87--92",
journal = "Analytical Biochemistry",
issn = "0003-2697",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Protein crosslinking reagents containing a selenoethylene linker are cleaved by mild oxidation

AU - Buchardt, O

AU - Elsner, H.

AU - Nielsen, Peter E.

AU - Petersen, L C

AU - Suenson, E.

PY - 1986/10

Y1 - 1986/10

N2 - A homobifunctional cleavable crosslinking reagent containing a selenoethylene group in the linker, and related reagents, have been synthesized and tested in a model system involving formation of a complex between albumin and cytochrome c. Functionally, complex formation was suggested by albumin inhibition of the ascorbate reduction of cytochrome c. Structurally, complex formation was demonstrated by crosslinking and subsequent separation of crosslinked complex from non-crosslinked proteins by SDS-polyacrylamide gel electrophoresis. The crosslinks were found to be cleavable by mild oxidation with low concentrations of periodate or with N-chlorobenzenesulfonamide immobilized on polystyrene beads (Iodo-Beads).

AB - A homobifunctional cleavable crosslinking reagent containing a selenoethylene group in the linker, and related reagents, have been synthesized and tested in a model system involving formation of a complex between albumin and cytochrome c. Functionally, complex formation was suggested by albumin inhibition of the ascorbate reduction of cytochrome c. Structurally, complex formation was demonstrated by crosslinking and subsequent separation of crosslinked complex from non-crosslinked proteins by SDS-polyacrylamide gel electrophoresis. The crosslinks were found to be cleavable by mild oxidation with low concentrations of periodate or with N-chlorobenzenesulfonamide immobilized on polystyrene beads (Iodo-Beads).

KW - Albumins

KW - Cross-Linking Reagents

KW - Cytochrome c Group

KW - Oxidation-Reduction

KW - Protein Binding

KW - Proteins

KW - Selenium

U2 - 10.1016/0003-2697(86)90593-2

DO - 10.1016/0003-2697(86)90593-2

M3 - Journal article

C2 - 3026203

VL - 158

SP - 87

EP - 92

JO - Analytical Biochemistry

JF - Analytical Biochemistry

SN - 0003-2697

IS - 1

ER -

ID: 203631687