Multiple isoforms of the human pentraxin serum amyloid P component.

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Standard

Multiple isoforms of the human pentraxin serum amyloid P component. / Sørensen, Inge Juul; Andersen, Ove; Nielsen, EH; Svehag, SE.

I: International Archives of Allergy and Immunology, Bind 106, Nr. 1, 1995, s. 25-31.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sørensen, IJ, Andersen, O, Nielsen, EH & Svehag, SE 1995, 'Multiple isoforms of the human pentraxin serum amyloid P component.', International Archives of Allergy and Immunology, bind 106, nr. 1, s. 25-31.

APA

Sørensen, I. J., Andersen, O., Nielsen, EH., & Svehag, SE. (1995). Multiple isoforms of the human pentraxin serum amyloid P component. International Archives of Allergy and Immunology, 106(1), 25-31.

Vancouver

Sørensen IJ, Andersen O, Nielsen EH, Svehag SE. Multiple isoforms of the human pentraxin serum amyloid P component. International Archives of Allergy and Immunology. 1995;106(1):25-31.

Author

Sørensen, Inge Juul ; Andersen, Ove ; Nielsen, EH ; Svehag, SE. / Multiple isoforms of the human pentraxin serum amyloid P component. I: International Archives of Allergy and Immunology. 1995 ; Bind 106, Nr. 1. s. 25-31.

Bibtex

@article{27dd9bb40a914fc4be8d9128eb763e1b,
title = "Multiple isoforms of the human pentraxin serum amyloid P component.",
abstract = "Human serum amyloid P component (SAP) isolated from 20 healthy individuals was analyzed by anion exchange chromatography and isoelectric focusing (IEF) in order to investigate the existence of multiple forms of SAP and interindividual structural differences. Anion exchange chromatography showed one major and several minor subpopulations of SAP. IEF of all SAP isolates showed a previously unreported degree of heterogeneity with six isoelectric forms (pKi range 5.5-6.1) and with minor interindividual differences in respect of isoelectric points. Total enzymatic deglycosylation of SAP reduced the number of bands in IEF to two indicating the existence of two types of polypeptide chains.",
author = "S{\o}rensen, {Inge Juul} and Ove Andersen and EH Nielsen and SE Svehag",
year = "1995",
language = "English",
volume = "106",
pages = "25--31",
journal = "International Archives of Allergy and Immunology",
issn = "1018-2438",
publisher = "S Karger AG",
number = "1",

}

RIS

TY - JOUR

T1 - Multiple isoforms of the human pentraxin serum amyloid P component.

AU - Sørensen, Inge Juul

AU - Andersen, Ove

AU - Nielsen, EH

AU - Svehag, SE

PY - 1995

Y1 - 1995

N2 - Human serum amyloid P component (SAP) isolated from 20 healthy individuals was analyzed by anion exchange chromatography and isoelectric focusing (IEF) in order to investigate the existence of multiple forms of SAP and interindividual structural differences. Anion exchange chromatography showed one major and several minor subpopulations of SAP. IEF of all SAP isolates showed a previously unreported degree of heterogeneity with six isoelectric forms (pKi range 5.5-6.1) and with minor interindividual differences in respect of isoelectric points. Total enzymatic deglycosylation of SAP reduced the number of bands in IEF to two indicating the existence of two types of polypeptide chains.

AB - Human serum amyloid P component (SAP) isolated from 20 healthy individuals was analyzed by anion exchange chromatography and isoelectric focusing (IEF) in order to investigate the existence of multiple forms of SAP and interindividual structural differences. Anion exchange chromatography showed one major and several minor subpopulations of SAP. IEF of all SAP isolates showed a previously unreported degree of heterogeneity with six isoelectric forms (pKi range 5.5-6.1) and with minor interindividual differences in respect of isoelectric points. Total enzymatic deglycosylation of SAP reduced the number of bands in IEF to two indicating the existence of two types of polypeptide chains.

M3 - Journal article

VL - 106

SP - 25

EP - 31

JO - International Archives of Allergy and Immunology

JF - International Archives of Allergy and Immunology

SN - 1018-2438

IS - 1

ER -

ID: 34097744