Structural similarities between C6 and C7 of human complement

E. R. Podack, W. P. Kolb, A. F. Esser, H. J. Muller-Eberhard

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

A new method for the isolation of C6 and C7 by affinity chromatography of human serum with anti-C6 and anti-C7 coupled to Sepharose is described. C6 and C7 prepared by this method are hemolytically fully active, homogeneous proteins obtained in 25% yield. A comparison of the properties of isolated C6 and C7 gave the following results: The amino acid composition of the two proteins is very similar. The m.w. calculated from the amino acid content is 124,800 for C6 and 120,800 for C7. Both components are single chain glycoproteins migrating upon electrophoresis at pH 8.6 as β2-globulins. Both proteins are polymorphic as detected by isoelectrofocusing in polyacrylamide gels and range in their isoelectric points from pH 6.15 to 6.7. The UV spectra reveal only minor differences; the extinction coefficients are: E(C6) = 1.71 cm2 x mg-1 and E(C7) = 1.92 cm2 x mg-1. CD-spectra show 8% α-helix and 10% β-structure for C6 and 10% α-helix and 14% β-structure for C7. The structural similarities of C6 and C7 suggest their evolution from a common ancestral gene.

Original languageEnglish
Pages (from-to)1071-1077
Number of pages7
JournalJournal of Immunology
Volume123
Issue number3
StatePublished - Jan 1 1979
Externally publishedYes

Fingerprint

Complement C7
Amino Acids
Proteins
Globulins
Isoelectric Point
Affinity Chromatography
Sepharose
Electrophoresis
Glycoproteins
Serum
Genes

ASJC Scopus subject areas

  • Immunology

Cite this

Podack, E. R., Kolb, W. P., Esser, A. F., & Muller-Eberhard, H. J. (1979). Structural similarities between C6 and C7 of human complement. Journal of Immunology, 123(3), 1071-1077.

Structural similarities between C6 and C7 of human complement. / Podack, E. R.; Kolb, W. P.; Esser, A. F.; Muller-Eberhard, H. J.

In: Journal of Immunology, Vol. 123, No. 3, 01.01.1979, p. 1071-1077.

Research output: Contribution to journalArticle

Podack, ER, Kolb, WP, Esser, AF & Muller-Eberhard, HJ 1979, 'Structural similarities between C6 and C7 of human complement', Journal of Immunology, vol. 123, no. 3, pp. 1071-1077.
Podack ER, Kolb WP, Esser AF, Muller-Eberhard HJ. Structural similarities between C6 and C7 of human complement. Journal of Immunology. 1979 Jan 1;123(3):1071-1077.
Podack, E. R. ; Kolb, W. P. ; Esser, A. F. ; Muller-Eberhard, H. J. / Structural similarities between C6 and C7 of human complement. In: Journal of Immunology. 1979 ; Vol. 123, No. 3. pp. 1071-1077.
@article{d23bea8e8d7e46f286f376b2b07b2e95,
title = "Structural similarities between C6 and C7 of human complement",
abstract = "A new method for the isolation of C6 and C7 by affinity chromatography of human serum with anti-C6 and anti-C7 coupled to Sepharose is described. C6 and C7 prepared by this method are hemolytically fully active, homogeneous proteins obtained in 25{\%} yield. A comparison of the properties of isolated C6 and C7 gave the following results: The amino acid composition of the two proteins is very similar. The m.w. calculated from the amino acid content is 124,800 for C6 and 120,800 for C7. Both components are single chain glycoproteins migrating upon electrophoresis at pH 8.6 as β2-globulins. Both proteins are polymorphic as detected by isoelectrofocusing in polyacrylamide gels and range in their isoelectric points from pH 6.15 to 6.7. The UV spectra reveal only minor differences; the extinction coefficients are: E(C6) = 1.71 cm2 x mg-1 and E(C7) = 1.92 cm2 x mg-1. CD-spectra show 8{\%} α-helix and 10{\%} β-structure for C6 and 10{\%} α-helix and 14{\%} β-structure for C7. The structural similarities of C6 and C7 suggest their evolution from a common ancestral gene.",
author = "Podack, {E. R.} and Kolb, {W. P.} and Esser, {A. F.} and Muller-Eberhard, {H. J.}",
year = "1979",
month = "1",
day = "1",
language = "English",
volume = "123",
pages = "1071--1077",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "3",

}

TY - JOUR

T1 - Structural similarities between C6 and C7 of human complement

AU - Podack, E. R.

AU - Kolb, W. P.

AU - Esser, A. F.

AU - Muller-Eberhard, H. J.

PY - 1979/1/1

Y1 - 1979/1/1

N2 - A new method for the isolation of C6 and C7 by affinity chromatography of human serum with anti-C6 and anti-C7 coupled to Sepharose is described. C6 and C7 prepared by this method are hemolytically fully active, homogeneous proteins obtained in 25% yield. A comparison of the properties of isolated C6 and C7 gave the following results: The amino acid composition of the two proteins is very similar. The m.w. calculated from the amino acid content is 124,800 for C6 and 120,800 for C7. Both components are single chain glycoproteins migrating upon electrophoresis at pH 8.6 as β2-globulins. Both proteins are polymorphic as detected by isoelectrofocusing in polyacrylamide gels and range in their isoelectric points from pH 6.15 to 6.7. The UV spectra reveal only minor differences; the extinction coefficients are: E(C6) = 1.71 cm2 x mg-1 and E(C7) = 1.92 cm2 x mg-1. CD-spectra show 8% α-helix and 10% β-structure for C6 and 10% α-helix and 14% β-structure for C7. The structural similarities of C6 and C7 suggest their evolution from a common ancestral gene.

AB - A new method for the isolation of C6 and C7 by affinity chromatography of human serum with anti-C6 and anti-C7 coupled to Sepharose is described. C6 and C7 prepared by this method are hemolytically fully active, homogeneous proteins obtained in 25% yield. A comparison of the properties of isolated C6 and C7 gave the following results: The amino acid composition of the two proteins is very similar. The m.w. calculated from the amino acid content is 124,800 for C6 and 120,800 for C7. Both components are single chain glycoproteins migrating upon electrophoresis at pH 8.6 as β2-globulins. Both proteins are polymorphic as detected by isoelectrofocusing in polyacrylamide gels and range in their isoelectric points from pH 6.15 to 6.7. The UV spectra reveal only minor differences; the extinction coefficients are: E(C6) = 1.71 cm2 x mg-1 and E(C7) = 1.92 cm2 x mg-1. CD-spectra show 8% α-helix and 10% β-structure for C6 and 10% α-helix and 14% β-structure for C7. The structural similarities of C6 and C7 suggest their evolution from a common ancestral gene.

UR - http://www.scopus.com/inward/record.url?scp=0018422866&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018422866&partnerID=8YFLogxK

M3 - Article

VL - 123

SP - 1071

EP - 1077

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 3

ER -