STEROID-PROTEIN INTERACTIONS. VIII. STRUCTURE OF DELTA (4)-3-KETOSTEROIDS IN RELATION TO SPECTROPHOTOMETRIC INTERACTION WITH HUMAN SERUM ALBUMIN

Abstract

Spectrophotometric observations show that introduction of methyl into delta (4)-3-ketosteroids strengthens the interaction with human serum albumin (HSA). Increase of the electron density at the rear side of the steroid molecule weakens this interaction. Simple alpha, beta-unsaturated ketones interact with HSA in a way similar to delta (4)-3-ketosteroids. The spectrometric results on the influence of functional groups in delta (4)-3-ketosteroids on interaction with HSA are summarized. Observation of bathochromic shifts in the ultraviolet absorption of 6 betamethyl-substituted delta (4)-3-ketosteroids confirms the concept of Ringold and Bowers that the inductive effect of a 6 beta-axial substituent is greater than that of the corresponding 6 alpha substituent. (Author)

Document Details

Document Type
Technical Report
Publication Date
Sep 20, 1961
Accession Number
AD0271068

Entities

People

  • Billy D. Ashley
  • Ulrich Westphal

Organizations

  • United States Army Medical Research Laboratory

Tags

DTIC Thesaurus Topics

  • Absorption
  • Albumins
  • Charged Particles
  • Electron Density
  • Electrons
  • Elementary Fermions
  • Elementary Particles
  • Fermions
  • Leptons
  • Molecules
  • Observation
  • Proteins
  • Steroids
  • Subatomic Particles

Fields of Study

  • Chemistry

Readers

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  • Organic Chemistry
  • Quantum Chemistry

Technology Areas

  • Microelectronics