FLOW BIREFRINGENCE STUDIES IN SOLUTIONS OF MACROMOLECULES

Abstract

Studies were made to determine the thermodynamic parameters characterizing the equilibria involved in the thrombin-induced fibrinogen-fibrin conversation. Peptide bonds, broken in the liberation of the polypeptide from the fibrinogen molecule, appeared much stronger than the usual bonds in simple peptides. Flow birefringence studies indicated the polymer distribution of activated fibrinogen below pH = 6 appeared of low molecular weight as compared to the high molecular weight of polymers between pH = 6 and 10. Flow birefringence and viscosity results suggested that the fibrinogen molecule may be split portions. Hydrodynamic and IR measurements identified the structural changes produced during the methylation of bovine serum albumin as esterifications of carboxyl groups. A quantitative correlation was obtained between the optical densities in the IR absorption spectra and the number of methoxyl groups.

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Document Details

Document Type
Technical Report
Publication Date
Jan 15, 1953
Accession Number
AD0006202

Entities

People

  • Harold A. Scheraga

Organizations

  • Cornell University

Tags

DTIC Thesaurus Topics

  • Absorption
  • Absorption Spectra
  • Albumins
  • Birefringence
  • Fibrinogen
  • Macromolecules
  • Military Research
  • Molecular Weight
  • Molecules
  • Polymers
  • Spectra

Fields of Study

  • Chemistry

Readers

  • Fluid Dynamics.
  • Molecular and Cellular Biochemistry
  • Spectroscopy.