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dc.creatorChao, Hsu
dc.descriptionDue to the character of the original source materials and the nature of batch digitization, quality control issues may be present in this document. Please report any quality issues you encounter to, referencing the URI of the item.en
dc.descriptionIncludes bibliographical references.en
dc.description.abstractA CDNA library representative of the S. mansoni egg MRNA populations was screened with rabbit anti-SEA antiserum and rabbit anti-GST antibody. Two of thirty-one positive clones were chosen for nucleotide sequencing and further study. A clone, SEA1, contains a 443 nucleotide sequence which encodes a 89 amino acid peptide sequence. The SEAL peptide sequence is highly homologous with members of the cystatin family 1. The other clone, SEA30, contains 1,140 nucleotides with a deduced peptide sequence of 343 amino acids. The SEA30 is highly homologous with the a-crystallin and small heat shock protein superfamily. The leucine aminopeptidase clone was obtained from the S. mansoni egg CDNA library by oligonucleotide screening. The LAP clone is a fragment of carboxyl half containing all the metal binding sites and structure characteristics found in other leucine aminopeptidases. The glutation S-transferases (GST) are enzymes that appear to play a central role in the parasitic detoxification system and have been shown to the important immunogens f or the elucidation of both protective and anti fecunidity immunity in schistosomiasis. For the purpose of preparing large quantities of recombinant material for immunilogical studies, Glutathion S-Transferase 26 (GST26) and Glutation S-Transferase 28 (GST28) were expressed through the procaryotic all purpose vector, pbluescript II. The yield of GST 26 was 20 mg from 1 liter cell culture. The yield of the GST 28 was 40 mg from 1 liter of cell culture. The GST 26 and GST 28 have been furthur identified by specific antibodies in western blot.en
dc.publisherTexas A&M University
dc.rightsThis thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries in 2008. Copyright remains vested with the author(s). It is the user's responsibility to secure permission from the copyright holder(s) for re-use of the work beyond the provision of Fair Use.en
dc.subjectveterinary parasitology.en
dc.subjectMajor veterinary parasitology.en
dc.titleMolecular cloning of Schistosoma mansoni egg cDNA clones of importance to host immune responseen
dc.typeThesisen parasitologyen
dc.format.digitalOriginreformatted digitalen

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