Accession Number:

ADA210310

Title:

Phenol Oxidase Mediated Protein Cross-Linking

Descriptive Note:

Annual rept. 1 Jun 1989

Corporate Author:

WYOMING UNIV LARAMIE

Personal Author(s):

• Cordingley, John S.
• Middaugh, C. R.

Report Date:

1989-06-26

Pagination or Media Count:

7.0

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 enzymes responsible for this process and to attempt to isolate, clone and sequence the genes for this enzymes. 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.

Descriptors:

• *PEPTIDES
• SCHISTOSOMA
• CALCIUM
• INFRARED SPECTROSCOPY
• SOLUTIONS(MIXTURES)
• WATER
• SECONDARY
• PROTEINS
• CROSSLINKING(CHEMISTRY)
• MOLECULAR STRUCTURE
• GENES
• CLONES
• MAPPING
• IN VIVO ANALYSIS
• FEMALES
• SCHISTOSOMA MANSONI
• TITRATION
• TANNING
• QUINONES
• COMPUTERIZED SIMULATION
• FOURIER TRANSFORMATION

Subject Categories:

• Genetic Engineering and Molecular Biology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE