Further characterization of a melanoma-specific protein from human urine

Isolation of a melanoma-specific protein (MSP) from human urine has been achieved using antibody affinity chromatography. MSP migrates as a single homogeneous protein on SDS PAGE and comparison of these data and ultracentrifuge analyses indicates that MSP contains a single polypeptide chain. MSP, ho...

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Bibliographic Details
Published in:British journal of cancer 1980-05, Vol.41 (5), p.734-744
Main Authors: Bennett, C, Cooke, K B
Format: Article
Language:English
Subjects:
alpha-Fetoproteins - immunology
Antibody Specificity
Antigens, Neoplasm - isolation & purification
Antigens, Neoplasm - urine
Biomedical and Life Sciences
Biomedicine
Cancer Research
Carcinoembryonic Antigen - immunology
Chromatography, Affinity
Drug Resistance
Electrophoresis, Polyacrylamide Gel
Epidemiology
Humans
Isoelectric Focusing
Melanoma - immunology
Melanoma - urine
Melanoma-Specific Antigens
Molecular Medicine
Molecular Weight
Neoplasm Proteins - urine
Oncology
original-article
Sialoglycoproteins - isolation & purification
Sialoglycoproteins - urine
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Summary:Isolation of a melanoma-specific protein (MSP) from human urine has been achieved using antibody affinity chromatography. MSP migrates as a single homogeneous protein on SDS PAGE and comparison of these data and ultracentrifuge analyses indicates that MSP contains a single polypeptide chain. MSP, however, shows considerable charge heterogeneity on isoelectric focusing. The desialo form, alpha 2 MSP, is found predominantly in patients with advanced metastatic disease, whilst only the sialo form alpha 1 MSP, is obtained from the urine of patients with early-stage disease. MSP does not react with antisera raised to alpha 1 foetoprotein (AFP) or carcinoembryonic antigen (CEA) and hence is immunologically distinct from these other tumour-associated glycoproteins. Antisera raised to MSP do not react with normal skin melanocytes nor with any foetal tissue tested, and hence the origin of MSP remains unresolved.
ISSN:0007-0920
1532-1827
DOI:10.1038/bjc.1980.135