Processing Enzyme Specificity is a Consequence of Pro-Hormone Precursor Protein Conformation,

Abstract

Gonadotropin associated peptide (GAP)-releasing enzyme and atrial granule serine proteinase (AGSP) which are isolated and purified from bovine hypothalamic neurosecretory granules and bovine atrial granules respectively, are likely processing enzymes of pro-gonadotropin-releasing hormone (Pro-Gn RH)/GAP and pro-atrial natriuretic factor (ANF) respectively. It was of interest to determine whether each enzyme would maintain its specificity when confronted with the processing sequence of the alternate enzyme. To this end, several peptides based on the primary sequency of pro-ANF and pro-GnRH/GAP were prepared which incorporated either the processing site sequence for the relevant enzyme for the processing site sequence for the alternate processing enzyme. Hydrolysis of these peptide substrates by both enzymes was then assessed.

Document Details

Document Type
Technical Report
Publication Date
Jan 01, 1992
Accession Number
ADP008367

Entities

People

  • N. S. Rangaraju
  • R. B. Harris

Organizations

  • Virginia Commonwealth University School of Medicine

Tags

DTIC Thesaurus Topics

  • Biomolecules
  • Chemical Compounds
  • Chemical Synthesis
  • Chemistry
  • Gonadotropins
  • Hormones
  • Hormones Hormone Substitutes And Hormone Antagonists
  • Hydrolysis
  • Massachusetts
  • Pituitary And Hypothalamic Hormones And Analogues
  • Precursors
  • Sequences
  • Substrates

Fields of Study

  • Biology

Readers

  • Cardiovascular Physiology
  • Molecular and Cellular Biochemistry