Linked Life Data

9136076

Source:http://linkedlifedata.com/resource/pubmed/id/9136076

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-6-19
pubmed:abstractText
PSP94 is a potential biomarker for evaluating patients with prostate carcinoma. We have systematically studied the epitope structure of PSP94 by using a polyclonal antibody against human PSP94. Results of peptide mapping and ELISA tests of dose response to rabbit antiserum against human PSP94 protein showed that only the N-terminal peptides (N30 and M23) are immunoreactive while all the synthetic peptides (C28, C10) located closer to the C-terminus are completely devoid of antigenic activity with the polyclonal antibody. These results were confirmed by analysis of reciprocal competitive binding of PSP94 polyclonal antibody by the N-terminal peptides (N30 and M23) v. either recombinant GST-PSP94 fusion protein, purified recombinant PSP94, or natural PSP94 protein. To further delineate the antigenic activity of the N- and C-termini, we have also expressed N- and C-terminal half of the whole PSP94 (each 47 peptides) using the E. coli GST expression system. The recombinant N47/C47 peptides were released by thrombin cleavage from the GST fusion protein and characterized by Western blotting experiments. Dose response of the recombinant GST-PSP-N47 and -C47 peptides to PSP94 polyclonal antibody showed differential binding activities. Competitive binding of these recombinant N47/C47 proteins against the GST-PSP94 protein demonstrates that the polyclonal antibody has a higher affinity for the N47 peptide than the C47 peptide. Based on the immunological studies of both synthetic peptides and recombinant PSP94- N/C terminal proteins, we propose an epitope structure of human PSP94 with an immuno-dominant N-terminus and an immuno-recessive C-terminus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0730-2312
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
172-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9136076-Amino Acid Sequence, pubmed-meshheading:9136076-Antibodies, pubmed-meshheading:9136076-Antigens, Neoplasm, pubmed-meshheading:9136076-Base Sequence, pubmed-meshheading:9136076-Binding, Competitive, pubmed-meshheading:9136076-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:9136076-Escherichia coli, pubmed-meshheading:9136076-Glutathione Transferase, pubmed-meshheading:9136076-Humans, pubmed-meshheading:9136076-Male, pubmed-meshheading:9136076-Molecular Sequence Data, pubmed-meshheading:9136076-Peptide Mapping, pubmed-meshheading:9136076-Prostatic Neoplasms, pubmed-meshheading:9136076-Prostatic Secretory Proteins, pubmed-meshheading:9136076-Proteins, pubmed-meshheading:9136076-Recombinant Fusion Proteins, pubmed-meshheading:9136076-Seminal Plasma Proteins, pubmed-meshheading:9136076-Tumor Markers, Biological
pubmed:year
1997
pubmed:articleTitle
Analysis of epitope structure of PSP94 (prostate secretory protein of 94 amino acids): (I). Immuno-dominant and immuno-recessive area.
pubmed:affiliation
Department of Surgery, University of Western Ontario, London, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't