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cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase.

M.1 monoclonal antibody has previously been shown to passively transfer partial resistance to schistosome infection within mice and to recognize a 28-kDa antigen that has peptide sequence homology with triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1). We hav...

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محفوظ في:
التفاصيل البيبلوغرافية
المؤلفون الرئيسيون: Shoemaker, C, Gross, A, Gebremichael, A, Harn, D
التنسيق: مقال
اللغة:en
منشور في: 1992
الموضوعات:
الوصول للمادة أونلاين:https://ncbi.nlm.nih.gov/pmc/articles/PMC48549/
https://ncbi.nlm.nih.gov/pubmed/1542681
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id pubmed-48549
record_format dspace
spelling pubmed-485492001-08-25 cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase. Shoemaker, C Gross, A Gebremichael, A Harn, D Proc Natl Acad Sci U S A Research Article M.1 monoclonal antibody has previously been shown to passively transfer partial resistance to schistosome infection within mice and to recognize a 28-kDa antigen that has peptide sequence homology with triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1). We have now isolated the complete coding DNA for Schistosoma mansoni TPI and confirmed that this cDNA encodes the 28-kDa antigen recognized by M.1. The predicted translation product has strong homology with other TPIs, particularly from higher eukaryotes, and the sequence homology is greatest in regions known to form the active site. The complete coding DNA has been expressed within an Escherichia coli host to produce high levels of soluble, recombinant S. mansoni TPI protein. The product is recognized and purified by the M.1 antibody and is a functional TPI with an intrinsic specific activity comparable to that of rabbit and yeast TPI. 1992-03-01 /pmc/articles/PMC48549/ /pubmed/1542681 Text en
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Research Article
spellingShingle Research Article
Shoemaker, C
Gross, A
Gebremichael, A
Harn, D
cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase.
description M.1 monoclonal antibody has previously been shown to passively transfer partial resistance to schistosome infection within mice and to recognize a 28-kDa antigen that has peptide sequence homology with triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1). We have now isolated the complete coding DNA for Schistosoma mansoni TPI and confirmed that this cDNA encodes the 28-kDa antigen recognized by M.1. The predicted translation product has strong homology with other TPIs, particularly from higher eukaryotes, and the sequence homology is greatest in regions known to form the active site. The complete coding DNA has been expressed within an Escherichia coli host to produce high levels of soluble, recombinant S. mansoni TPI protein. The product is recognized and purified by the M.1 antibody and is a functional TPI with an intrinsic specific activity comparable to that of rabbit and yeast TPI.
author Shoemaker, C
Gross, A
Gebremichael, A
Harn, D
author_facet Shoemaker, C
Gross, A
Gebremichael, A
Harn, D
author_sort Shoemaker, C
title cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase.
title_short cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase.
title_full cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase.
title_fullStr cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase.
title_full_unstemmed cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase.
title_sort cdna cloning and functional expression of the schistosoma mansoni protective antigen triose-phosphate isomerase.
publishDate 1992
url https://ncbi.nlm.nih.gov/pmc/articles/PMC48549/
https://ncbi.nlm.nih.gov/pubmed/1542681
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