Phenol Oxidase Mediated Protein Cross-Linking
Abstract
The aim of this research is to investigate the secondary structure of the highly repetitive schistosome eggshell protein known in our laboratory as F4. The schistosome eggshell is cross-linked by 'quinone tanning' apparently catalyzed by a copper dependent phenol oxidase and a secondary aim of this project is to characterize the enzyme(s) responsible for this process and to attempt to isolate, clone and sequence the genes for this enzyme(s). We are attempting to determine the secondary structure of the repetitive eggshell protein from Schistosoma mansoni using synthetic peptides. CD spectroscopy, Fourier transform Infra-red spectroscopy, titration experiments and computer modeling, all suggest that this protein adopts a left-handed alpha-helix in aqueous solution, the first time such a structure has been reported in a natural protein. Experiments in vivo suggest that pH and calcium play important roles in regulating the polymerization of schistosome eggshell. We have developed a novel method for detecting DOPA proteins. These proteins are only found in the vitellaria of mature female schistosomes. Keywords: Gene sequencing; Gene mapping; Clones.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 26, 1989
- Accession Number
- ADA210310
Entities
People
- C. R. Middaugh
- John S. Cordingley
Organizations
- University of Wyoming