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Isolation of component C4 of human complement and its polypeptide chains

Lundwall, Åke LU ; Malmheden, I.; Stalenheim, G. and Sjoquist, J. (1981) In Eur J Biochem 117(1). p.6-141
Abstract
Component C4 of human complement was purified from fresh frozen plasma with a yield of 25% using an initial batch separation with quaternary diethyl-(2-hydroxypropyl)aminoethyl--Sephadex followed by column chromatography on DEAE-cellulose and gel filtration in Sephadex G-200. The final product was homogenous according to polyacrylamide gel electrophoresis and immunochemical methods. Low-speed sedimentation-equilibrium analyses revealed a molecular weight of 189,000, using a value of 0.736 ml/g for the partial specific volume. The polypeptide chains of reduced and alkylated C4 were separated on DEAE-Sepharose in the presence of 8 M urea. Gel filtration in Sepharose 4B in 6 M guanidine hydrochloride revealed molecular weights of 88,000,... (More)
Component C4 of human complement was purified from fresh frozen plasma with a yield of 25% using an initial batch separation with quaternary diethyl-(2-hydroxypropyl)aminoethyl--Sephadex followed by column chromatography on DEAE-cellulose and gel filtration in Sephadex G-200. The final product was homogenous according to polyacrylamide gel electrophoresis and immunochemical methods. Low-speed sedimentation-equilibrium analyses revealed a molecular weight of 189,000, using a value of 0.736 ml/g for the partial specific volume. The polypeptide chains of reduced and alkylated C4 were separated on DEAE-Sepharose in the presence of 8 M urea. Gel filtration in Sepharose 4B in 6 M guanidine hydrochloride revealed molecular weights of 88,000, 72,000 and 32,000 for the alpha, beta and gamma chain respectively. The amino acid compositions of component C4 and its constitutive chains were also determined. (Less)
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published
subject
keywords
Macromolecular Substances, Immune Sera, Humans, Guanidines, Guanidine, Amino Acids/analysis, Complement C4/*isolation & purification, Molecular Weight, Research Support, Non-U.S. Gov't
in
Eur J Biochem
volume
117
issue
1
pages
6 - 141
external identifiers
  • Scopus:0019795755
language
English
LU publication?
no
id
a0ffd06b-76a9-44a6-b79d-3ce7841493ee (old id 3965012)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7262082
date added to LUP
2013-08-11 18:32:47
date last changed
2016-10-13 04:54:06
@misc{a0ffd06b-76a9-44a6-b79d-3ce7841493ee,
  abstract     = {Component C4 of human complement was purified from fresh frozen plasma with a yield of 25% using an initial batch separation with quaternary diethyl-(2-hydroxypropyl)aminoethyl--Sephadex followed by column chromatography on DEAE-cellulose and gel filtration in Sephadex G-200. The final product was homogenous according to polyacrylamide gel electrophoresis and immunochemical methods. Low-speed sedimentation-equilibrium analyses revealed a molecular weight of 189,000, using a value of 0.736 ml/g for the partial specific volume. The polypeptide chains of reduced and alkylated C4 were separated on DEAE-Sepharose in the presence of 8 M urea. Gel filtration in Sepharose 4B in 6 M guanidine hydrochloride revealed molecular weights of 88,000, 72,000 and 32,000 for the alpha, beta and gamma chain respectively. The amino acid compositions of component C4 and its constitutive chains were also determined.},
  author       = {Lundwall, Åke and Malmheden, I. and Stalenheim, G. and Sjoquist, J.},
  keyword      = {Macromolecular Substances,Immune Sera,Humans,Guanidines,Guanidine,Amino Acids/analysis,Complement C4/*isolation & purification,Molecular Weight,Research Support,Non-U.S. Gov't},
  language     = {eng},
  number       = {1},
  pages        = {6--141},
  series       = {Eur J Biochem},
  title        = {Isolation of component C4 of human complement and its polypeptide chains},
  volume       = {117},
  year         = {1981},
}