Antibodies to the unfolded form of a helix-rich region in staphylococcal nuclease

Bruce Furie, Alan N. Schechter, David H. Sachs, Christian B. Anfinsen

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16 Scopus citations

Abstract

Goat antibodies prepared against a polypeptide fragment of staphylococcal nuclease, (99-149), have been fractionated by affinity chromatography to yield a population of antibodies specific for the region of amino acid residues 99-126 of nuclease. These anti-(99-126)R antibodies do not precipitate with nuclease or with. (99-149) and are operationally monospecific, as inferred from sedimentation velocity ultracentrifugation studies, for a distinct antigenic determinant on fragment (99-149). The anti-(99-126)R antibody populations are heterogeneous with regard to charge but show some restrictions as compared to anti-(99-149)R in disc gel electrophoresis and isoelectric focusing experiments. Binding data for the interaction of (99-149) and anti-(99-126)R antibodies, analyzed using a Scatchard plot, suggested that the antibodies were composed of a high affinity population with an average Kisa of 1.2 ×107M-1 and a lower affinity population with an average Kass of 1 × 106M-1. Purification and characterization of this antibody population will facilitate the study of the conformational equilibrium of native nuclease.

Original languageEnglish
Pages (from-to)1561-1566
Number of pages6
JournalBiochemistry
Volume13
Issue number8
DOIs
StatePublished - 1 Apr 1974
Externally publishedYes

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