Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production

A. F. Strachan; E. G. Shephard; D. U. Bellstedt; G. A. Coetzee; D. R. Van Der Westhuyzen; F. C. De Beer

doi:10.1042/bj2630365

Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production

A. F. Strachan, E. G. Shephard, D. U. Bellstedt, G. A. Coetzee, D. R. Van Der Westhuyzen, F. C. De Beer

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

19 Scopus citations

Abstract

Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (>90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at >7 M-urea. By immunizing with apo-SAA adsorbed to acid treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.

Original language	English
Pages (from-to)	365-370
Number of pages	6
Journal	Biochemical Journal
Volume	263
Issue number	2
DOIs	https://doi.org/10.1042/bj2630365
State	Published - 1989

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production",

abstract = "Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (>90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at >7 M-urea. By immunizing with apo-SAA adsorbed to acid treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.",

author = "Strachan, {A. F.} and Shephard, {E. G.} and Bellstedt, {D. U.} and Coetzee, {G. A.} and {Van Der Westhuyzen}, {D. R.} and {De Beer}, {F. C.}",

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AU - Strachan, A. F.

AU - Shephard, E. G.

AU - Bellstedt, D. U.

AU - Coetzee, G. A.

AU - Van Der Westhuyzen, D. R.

AU - De Beer, F. C.

PY - 1989

Y1 - 1989

N2 - Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (>90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at >7 M-urea. By immunizing with apo-SAA adsorbed to acid treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.

AB - Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (>90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at >7 M-urea. By immunizing with apo-SAA adsorbed to acid treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.

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Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production

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