Literature DB >> 19871481

STUDIES ON THE DENATURATION OF ANTIBODY : II. THE EFFECT OF PROTEIN CONCENTRATION ON THE RATE OF DENATURATION OF DIPHTHERIA ANTITOXIN BY UREA.

G G Wright1.   

Abstract

The specific rate of inactivation of antitoxin in urea solutions, as measured by the Römer neutralization test with toxin, has been shown to be independent of the concentration of protein under the conditions studied. The amount of precipitate obtained in the quantitative precipitation test with toxin, however, increases greatly with increasing protein concentration during denaturation. The time during which the protein concentration is important in this respect has been shown to be the interval in which the urea is being dialyzed from the solutions. The meaning of the results is discussed.

Entities:  

Year:  1945        PMID: 19871481      PMCID: PMC2135519          DOI: 10.1084/jem.81.6.647

Source DB:  PubMed          Journal:  J Exp Med        ISSN: 0022-1007            Impact factor:   14.307


  4 in total

1.  The effect of salts on the formation of protein complexes during heat denaturation.

Authors:  A Kleczkowski
Journal:  Biochem J       Date:  1943-04       Impact factor: 3.857

2.  A NOTE ON THE SEROLOGICAL ACTIVITY OF DENATURED ANTIBODIES.

Authors:  G G Wright; L Pauling
Journal:  Science       Date:  1944-03-10       Impact factor: 47.728

3.  STUDIES ON PHOTO-OXIDATION OF ANTIGEN AND ANTIBODIES.

Authors:  H Smetana; D Shemin
Journal:  J Exp Med       Date:  1941-01-31       Impact factor: 14.307

4.  STUDIES ON THE DENATURATION OF ANTIBODY : I. THE ACTION OF UREA ON DIPHTHERIA ANTITOXIN.

Authors:  G G Wright
Journal:  J Exp Med       Date:  1944-04-01       Impact factor: 14.307

  4 in total
  1 in total

1.  THE EFFECT OF HIGH PRESSURES ON HEMAGGLUTINATING ANTIBODIES.

Authors:  W C Boyd
Journal:  J Exp Med       Date:  1946-04-30       Impact factor: 14.307

  1 in total

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