Native human serum amyloid P component is a single pentamer

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Standard

Native human serum amyloid P component is a single pentamer. / Sørensen, Inge Juul; Andersen, Ove; Nielsen, EH; Svehag, SE.

I: Scandinavian Journal of Immunology, Bind 41, Nr. 3, 1995, s. 263-7.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sørensen, IJ, Andersen, O, Nielsen, EH & Svehag, SE 1995, 'Native human serum amyloid P component is a single pentamer', Scandinavian Journal of Immunology, bind 41, nr. 3, s. 263-7.

APA

Sørensen, I. J., Andersen, O., Nielsen, EH., & Svehag, SE. (1995). Native human serum amyloid P component is a single pentamer. Scandinavian Journal of Immunology, 41(3), 263-7.

Vancouver

Sørensen IJ, Andersen O, Nielsen EH, Svehag SE. Native human serum amyloid P component is a single pentamer. Scandinavian Journal of Immunology. 1995;41(3):263-7.

Author

Sørensen, Inge Juul ; Andersen, Ove ; Nielsen, EH ; Svehag, SE. / Native human serum amyloid P component is a single pentamer. I: Scandinavian Journal of Immunology. 1995 ; Bind 41, Nr. 3. s. 263-7.

Bibtex

@article{0fe1e919f2574018ad14c47db60f10b8,
title = "Native human serum amyloid P component is a single pentamer",
abstract = "Serum amyloid P component (SAP) and C-reactive protein (CRP) are members of the pentraxin protein family. SAP is the precursor protein to amyloid P component present in all forms of amyloidosis. The prevailing notion is that SAP in circulation has the form of a double pentameric molecule (decamer) whereas CRP is a single pentameric molecule. We have investigated by gel permeation chromatography the M(r) of SAP in freshly collected human serum and of SAP purified by carbohydrate affinity chromatography and anion exchange chromatography. SAP was monitored by quantitative immunoelectrophoresis and ELISA, and SAP peak fractions were analysed by use of SDS-PAGE, Western blotting, and electron microscopy. The results indicate that native SAP circulates as a single pentamer, a part of which forms complexes with C4b-binding protein. The properties of SAP changed during purification as indicated by rocket immunoelectrophoresis and electron microscopy. Thus, electron micrographs of purified SAP showed a predominance of decamers. However, the decamer form of SAP reversed to single pentamers when purified SAP was incorporated into SAP-depleted serum.",
author = "S{\o}rensen, {Inge Juul} and Ove Andersen and EH Nielsen and SE Svehag",
year = "1995",
language = "English",
volume = "41",
pages = "263--7",
journal = "Scandinavian Journal of Immunology, Supplement",
issn = "0301-6323",
publisher = "Wiley-Blackwell",
number = "3",

}

RIS

TY - JOUR

T1 - Native human serum amyloid P component is a single pentamer

AU - Sørensen, Inge Juul

AU - Andersen, Ove

AU - Nielsen, EH

AU - Svehag, SE

PY - 1995

Y1 - 1995

N2 - Serum amyloid P component (SAP) and C-reactive protein (CRP) are members of the pentraxin protein family. SAP is the precursor protein to amyloid P component present in all forms of amyloidosis. The prevailing notion is that SAP in circulation has the form of a double pentameric molecule (decamer) whereas CRP is a single pentameric molecule. We have investigated by gel permeation chromatography the M(r) of SAP in freshly collected human serum and of SAP purified by carbohydrate affinity chromatography and anion exchange chromatography. SAP was monitored by quantitative immunoelectrophoresis and ELISA, and SAP peak fractions were analysed by use of SDS-PAGE, Western blotting, and electron microscopy. The results indicate that native SAP circulates as a single pentamer, a part of which forms complexes with C4b-binding protein. The properties of SAP changed during purification as indicated by rocket immunoelectrophoresis and electron microscopy. Thus, electron micrographs of purified SAP showed a predominance of decamers. However, the decamer form of SAP reversed to single pentamers when purified SAP was incorporated into SAP-depleted serum.

AB - Serum amyloid P component (SAP) and C-reactive protein (CRP) are members of the pentraxin protein family. SAP is the precursor protein to amyloid P component present in all forms of amyloidosis. The prevailing notion is that SAP in circulation has the form of a double pentameric molecule (decamer) whereas CRP is a single pentameric molecule. We have investigated by gel permeation chromatography the M(r) of SAP in freshly collected human serum and of SAP purified by carbohydrate affinity chromatography and anion exchange chromatography. SAP was monitored by quantitative immunoelectrophoresis and ELISA, and SAP peak fractions were analysed by use of SDS-PAGE, Western blotting, and electron microscopy. The results indicate that native SAP circulates as a single pentamer, a part of which forms complexes with C4b-binding protein. The properties of SAP changed during purification as indicated by rocket immunoelectrophoresis and electron microscopy. Thus, electron micrographs of purified SAP showed a predominance of decamers. However, the decamer form of SAP reversed to single pentamers when purified SAP was incorporated into SAP-depleted serum.

M3 - Journal article

VL - 41

SP - 263

EP - 267

JO - Scandinavian Journal of Immunology, Supplement

JF - Scandinavian Journal of Immunology, Supplement

SN - 0301-6323

IS - 3

ER -

ID: 34098093