A simplified method for purification of human C5a from citrated plasma

Lois Renfer; Michael M. Frank; Carl H. Hammer; Liana Harvath; Thomas J. Lawley; Kim B. Yancey

doi:10.1016/0022-1759(86)90006-2

A simplified method for purification of human C5a from citrated plasma

Lois Renfer, Michael M. Frank, Carl H. Hammer, Liana Harvath, Thomas J. Lawley, Kim B. Yancey

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

A simplified immunoadsorption technique has been developed to purify human C5a, the 11 000 Da glycopeptide produced by C5 convertase cleavage of the fifth component of complement. In this method, human C5 fragments, including C5a, are isolated from zymosan-activated plasma by affinity chromatography, concentrated on CM 52 cellulose, and then purified to homogeneity by gel filtration on Sephadex G-75 in phosphate-buffered saline. Human C5a prepared by this technique demonstrates characteristic immunochemical and biologic activity. This method has also been adapted for the purification of ¹²⁵I-C5a in phosphate-buffered saline. This technique offers a simplified approach to the purification of this important soluble mediator of inflammation.

Original language	English (US)
Pages (from-to)	193-205
Number of pages	13
Journal	Journal of Immunological Methods
Volume	88
Issue number	2
DOIs	https://doi.org/10.1016/0022-1759(86)90006-2
State	Published - Apr 17 1986

Keywords

Anaphylatoxin purification
Complement
Human C5a

ASJC Scopus subject areas

Immunology and Allergy
Immunology

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10.1016/0022-1759(86)90006-2

Cite this

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title = "A simplified method for purification of human C5a from citrated plasma",

abstract = "A simplified immunoadsorption technique has been developed to purify human C5a, the 11 000 Da glycopeptide produced by C5 convertase cleavage of the fifth component of complement. In this method, human C5 fragments, including C5a, are isolated from zymosan-activated plasma by affinity chromatography, concentrated on CM 52 cellulose, and then purified to homogeneity by gel filtration on Sephadex G-75 in phosphate-buffered saline. Human C5a prepared by this technique demonstrates characteristic immunochemical and biologic activity. This method has also been adapted for the purification of 125I-C5a in phosphate-buffered saline. This technique offers a simplified approach to the purification of this important soluble mediator of inflammation.",

keywords = "Anaphylatoxin purification, Complement, Human C5a",

author = "Lois Renfer and Frank, {Michael M.} and Hammer, {Carl H.} and Liana Harvath and Lawley, {Thomas J.} and Yancey, {Kim B.}",

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T1 - A simplified method for purification of human C5a from citrated plasma

AU - Renfer, Lois

AU - Frank, Michael M.

AU - Hammer, Carl H.

AU - Harvath, Liana

AU - Lawley, Thomas J.

AU - Yancey, Kim B.

PY - 1986/4/17

Y1 - 1986/4/17

N2 - A simplified immunoadsorption technique has been developed to purify human C5a, the 11 000 Da glycopeptide produced by C5 convertase cleavage of the fifth component of complement. In this method, human C5 fragments, including C5a, are isolated from zymosan-activated plasma by affinity chromatography, concentrated on CM 52 cellulose, and then purified to homogeneity by gel filtration on Sephadex G-75 in phosphate-buffered saline. Human C5a prepared by this technique demonstrates characteristic immunochemical and biologic activity. This method has also been adapted for the purification of 125I-C5a in phosphate-buffered saline. This technique offers a simplified approach to the purification of this important soluble mediator of inflammation.

AB - A simplified immunoadsorption technique has been developed to purify human C5a, the 11 000 Da glycopeptide produced by C5 convertase cleavage of the fifth component of complement. In this method, human C5 fragments, including C5a, are isolated from zymosan-activated plasma by affinity chromatography, concentrated on CM 52 cellulose, and then purified to homogeneity by gel filtration on Sephadex G-75 in phosphate-buffered saline. Human C5a prepared by this technique demonstrates characteristic immunochemical and biologic activity. This method has also been adapted for the purification of 125I-C5a in phosphate-buffered saline. This technique offers a simplified approach to the purification of this important soluble mediator of inflammation.

KW - Anaphylatoxin purification

KW - Complement

KW - Human C5a

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A simplified method for purification of human C5a from citrated plasma

Abstract

Keywords

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