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May 1, 1968Biochemistry

The covalent structure of a human γG-immunoglobulin. III. Arrangement of the cyanogen bromide fragments

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Authors

MWMyron J. WaxdalRutgers, The State University of New JerseyWKWilliam H. KonigsbergYale UniversityGEGerald M. EdelmanRockefeller Foundation

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Implication

Research examines the structural arrangement of cyanogen bromide fragments in human γG-immunoglobulin, highlighting key interactions.

Key Points

  • The aim is to elucidate the covalent structure and fragment arrangement of human γG-immunoglobulin.
  • Analyzed the covalent structure of γG-immunoglobulin using cyanogen bromide cleavage.
  • Investigated fragment arrangements produced by the cyanogen bromide treatment.
  • Characterized the specific arrangement of cyanogen bromide fragments within the immunoglobulin structure.
  • Detailed multiple covalent interactions between fragments showing their precise orientations.

Cite This Study

Waxdal et al. (1968) studied this question.

synapsesocial.com/papers/6a1bfb294ebd09f3dfa94a75https://doi.org/10.1021/bi00845a047
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The covalent structure of a human γG-immunoglobulin. II. Isolation and characterization of the cyanogen bromide fragments1968 · 172 citations
  2. 2The covalent structure of a human γG-immunoglobulin. I. Isolation and characterization of the whole molecule, the polypeptide chains, and the tryptic fragments1968 · 115 citations
  3. 3Chromatographic Separation of Peptides on Ion Exchange Resins. Separation of Peptides from Enzymatic Hydrolyzates of the α,β, and γ Chains of Human Hemoglobins.1962 · 219 citations
  4. 4The chemical structure of the heavy chains of rabbit and human immunoglobulin G (IgG)1966 · 23 citations
  5. 5Automatic Method for Separation, Hydrolysis, and Detection of Peptides.1964 · 56 citations