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. 1939 Jan 1;69(1):103–118. doi: 10.1084/jem.69.1.103

THE MOLECULAR WEIGHT OF ANTIBODIES

Elvin A Kabat 1
PMCID: PMC2133729  PMID: 19870830

Abstract

1. Highly purified preparations of homogeneous antibody can be made by the salt dissociation methods (6, 7) without any change in sedimentation due to the method of purification. 2. Antibodies prepared from sera of various animal species fall into two groups as regards molecular weight; in one group cow, horse, and pig, a heavy molecule of molecular weight 990,000 is formed; in human being, rabbit, and monkey, the molecular size is that of the normal γ serum globulin. Both types of antibody molecules are either not compact or not spherical since the frictional ratios f/f 0 are 2.0 and 1.5 respectively. 3. Horse antibody shows an unchanged activity and sedimentation diagram between pH 3.44–9.06, although there is some aggregation at the more acid and some dissociation at the more alkaline pH. At pH 1.44 the antibody activity is unchanged but some breakdown of the molecule takes place. At pH 12.4 activity is destroyed and the molecule is completely broken down. 4. Some horse antibody preparations show evidence of breakdown of the antibody into inhomogeneous material on continued immunization over a long period.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Heidelberger M., Kabat E. A. CHEMICAL STUDIES ON BACTERIAL AGGLUTINATION : I. A METHOD. J Exp Med. 1934 Oct 31;60(5):643–653. doi: 10.1084/jem.60.5.643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Heidelberger M., Kabat E. A. CHEMICAL STUDIES ON BACTERIAL AGGLUTINATION : II. THE IDENTITY OF PRECIPITIN AND AGGLUTININ. J Exp Med. 1936 Apr 30;63(5):737–744. doi: 10.1084/jem.63.5.737. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Heidelberger M., Kabat E. A. QUANTITATIVE STUDIES ON ANTIBODY PURIFICATION : II. THE DISSOCIATION OF ANTIBODY FROM PNEUMOCOCCUS SPECIFIC PRECIPITATES AND SPECIFICALLY AGGLUTINATED PNEUMOCOCCI. J Exp Med. 1938 Jan 31;67(2):181–199. doi: 10.1084/jem.67.2.181. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Heidelberger M., Kendall F. E. QUANTITATIVE STUDIES ON ANTIBODY PURIFICATION : I. THE DISSOCIATION OF PRECIPITATES FORMED BY PNEUMOCOCCUS SPECIFIC POLYSACCHARIDES AND HOMOLOGOUS ANTIBODIES. J Exp Med. 1936 Jul 31;64(2):161–172. doi: 10.1084/jem.64.2.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Heidelberger M., Kendall F. E. STUDIES ON THE PRECIPITIN REACTION : PRECIPITATING HAPTENS; SPECIES DIFFERENCES IN ANTIBODIES. J Exp Med. 1933 Feb 28;57(3):373–379. doi: 10.1084/jem.57.3.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Heidelberger M., Kendall F. E., Scherp H. W. THE SPECIFIC POLYSACCHARIDES OF TYPES I, II, AND III PNEUMOCOCCUS : A REVISION OF METHODS AND DATA. J Exp Med. 1936 Sep 30;64(4):559–572. doi: 10.1084/jem.64.4.559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Heidelberger M., Kendall F. E. THE PRECIPITIN REACTION BETWEEN TYPE III PNEUMOCOCCUS POLYSACCHARIDE AND HOMOLOGOUS ANTIBODY : II. CONDITIONS FOR QUANTITATIVE PRECIPITATION OF ANTIBODY IN HORSE SERA. J Exp Med. 1935 Mar 31;61(4):559–562. doi: 10.1084/jem.61.4.559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Heidelberger M., Pedersen K. O. THE MOLECULAR WEIGHT OF ANTIBODIES. J Exp Med. 1937 Feb 28;65(3):393–414. doi: 10.1084/jem.65.3.393. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Heidelberger M., Sia R. H., Kendall F. E. SPECIFIC PRECIPITATION AND MOUSE PROTECTION IN TYPE I ANTIPNEUMOCOCCUS SERA. J Exp Med. 1930 Sep 30;52(4):477–483. doi: 10.1084/jem.52.4.477. [DOI] [PMC free article] [PubMed] [Google Scholar]

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