The murine monoclonal antibodies (MAb) TURP-27 and HNK-1 have been shown to detect antigens that are heavily expressed by benign prostatic hyperplasia (BPH) and carcinoma of the prostate (CaP). Western blot analysis of prostate extracts, showed that MAb TURP-27 and MAb HNK-1 bound glycoproteins of 180, 140, 120, 100, 90 and 69 kDa. Studies have shown that the HNK-1 carbohydrate epitope may be involved in cell adhesion and that it is a component of several characterized adhesion proteins. TURP-27 was found to bind at least three of these adhesion proteins: neural cell adhesion molecules (N-CAM), myelin-associated glycoprotein (MAG) and a second myelin glycoprotein, P0. Western blot analysis of prostate extracts showed that an anti-N-CAM serum bound the 180 and 140 kDa proteins. On the basis of reciprocal blocking and chemical tests, it was determined that the TURP-27 and HNK-1 epitopes are not identical. These data imply that the TURP-27 epitope may be a variant of the HNK-1 epitope or that the two epitopes are closely linked, and that the TURP-27 and HNK-1 epitopes on prostate cells are positioned on N-CAM like proteins.
","abstract_html":"<p>The murine monoclonal antibodies (MAb) TURP-27 and HNK-1 have been shown to detect antigens that are heavily expressed by benign prostatic hyperplasia (BPH) and carcinoma of the prostate (CaP). Western blot analysis of prostate extracts, showed that MAb TURP-27 and MAb HNK-1 bound glycoproteins of 180, 140, 120, 100, 90 and 69 kDa. Studies have shown that the HNK-1 carbohydrate epitope may be involved in cell adhesion and that it is a component of several characterized adhesion proteins. TURP-27 was found to bind at least three of these adhesion proteins: neural cell adhesion molecules (N-CAM), myelin-associated glycoprotein (MAG) and a second myelin glycoprotein, P<sub>0</sub>. Western blot analysis of prostate extracts showed that an anti-N-CAM serum bound the 180 and 140 kDa proteins. On the basis of reciprocal blocking and chemical tests, it was determined that the TURP-27 and HNK-1 epitopes are not identical. These data imply that the TURP-27 epitope may be a variant of the HNK-1 epitope or that the two epitopes are closely linked, and that the TURP-27 and HNK-1 epitopes on prostate cells are positioned on N-CAM like proteins.</p>","abstract_has_math":false,"creators":["Lipford, Grayson B."],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Biological Sciences","degree_department":null,"school":null,"contributors":["George L. Wright, Jr.","Kenneth D. Somers","Gary F. Clark","Robert E. Ratzlaff"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1992,"date_issued":"1992-04-01T08:00:00Z","date_published":"1992-04-01T08:00:00Z","updated_at":"2026-07-24T03:35:15Z","subjects":["HNK-1","TURP-27","Prostate tumor","Antigen","Cell Biology","Medical Immunology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.odu.edu/biomedicalsciences_etds/125","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["George L. Wright, Jr.","Kenneth D. Somers","Gary F. Clark","Robert E. Ratzlaff"]},{"key":"dc:creator","label":"Author","values":["Lipford, Grayson B."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2019-10-02T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biological Sciences"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["HNK-1","TURP-27","Prostate tumor","Antigen","Cell Biology","Medical Immunology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalcommons.odu.edu/biomedicalsciences_etds/125"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The murine monoclonal antibodies (MAb) TURP-27 and HNK-1 have been shown to detect antigens that are heavily expressed by benign prostatic hyperplasia (BPH) and carcinoma of the prostate (CaP). Western blot analysis of prostate extracts, showed that MAb TURP-27 and MAb HNK-1 bound glycoproteins of 180, 140, 120, 100, 90 and 69 kDa. Studies have shown that the HNK-1 carbohydrate epitope may be involved in cell adhesion and that it is a component of several characterized adhesion proteins. TURP-27 was found to bind at least three of these adhesion proteins: neural cell adhesion molecules (N-CAM), myelin-associated glycoprotein (MAG) and a second myelin glycoprotein, P0. Western blot analysis of prostate extracts showed that an anti-N-CAM serum bound the 180 and 140 kDa proteins. On the basis of reciprocal blocking and chemical tests, it was determined that the TURP-27 and HNK-1 epitopes are not identical. These data imply that the TURP-27 epitope may be a variant of the HNK-1 epitope or that the two epitopes are closely linked, and that the TURP-27 and HNK-1 epitopes on prostate cells are positioned on N-CAM like proteins.
"]},{"key":"dc:title","label":"Title","values":["Characterization of a Novel Prostate Tumor-Associated Antigen"]}]}],"canonical_facts":{"dc:contributor":["George L. Wright, Jr.","Kenneth D. Somers","Gary F. Clark","Robert E. Ratzlaff"],"dc:creator":["Lipford, Grayson B."],"dc:date.available":["2019-10-02T07:00:00Z"],"dc:description.abstract":["The murine monoclonal antibodies (MAb) TURP-27 and HNK-1 have been shown to detect antigens that are heavily expressed by benign prostatic hyperplasia (BPH) and carcinoma of the prostate (CaP). Western blot analysis of prostate extracts, showed that MAb TURP-27 and MAb HNK-1 bound glycoproteins of 180, 140, 120, 100, 90 and 69 kDa. Studies have shown that the HNK-1 carbohydrate epitope may be involved in cell adhesion and that it is a component of several characterized adhesion proteins. TURP-27 was found to bind at least three of these adhesion proteins: neural cell adhesion molecules (N-CAM), myelin-associated glycoprotein (MAG) and a second myelin glycoprotein, P0. Western blot analysis of prostate extracts showed that an anti-N-CAM serum bound the 180 and 140 kDa proteins. On the basis of reciprocal blocking and chemical tests, it was determined that the TURP-27 and HNK-1 epitopes are not identical. These data imply that the TURP-27 epitope may be a variant of the HNK-1 epitope or that the two epitopes are closely linked, and that the TURP-27 and HNK-1 epitopes on prostate cells are positioned on N-CAM like proteins.
"],"dc:identifier":["https://digitalcommons.odu.edu/biomedicalsciences_etds/125"],"dc:subject":["HNK-1","TURP-27","Prostate tumor","Antigen","Cell Biology","Medical Immunology"],"dc:title":["Characterization of a Novel Prostate Tumor-Associated Antigen"],"thesis:degree_discipline":["Biological Sciences"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T03:35:15Z"}