Purification and characterization of prostate specific antigen from human urine

Prostate specific antigen (uPSA) was purified to homogeneity from human urine using SuperQ-Toyopearl, Sulfate-Cellulofine, Phenyl-Toyopearl, CM-Sepharose, anti-urokinase IgG Sepharose and Sephadex G-100. The purified uPSA gave a major band at 32.9 kDa on SDS-PAGE under the reduced condition. However...

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Bibliographic Details
Published in:Biochimica et biophysica acta 1997-10, Vol.1336 (3), p.425-433
Main Authors: Shibata, Kozue, Kajihara, Jun-ichi, Kato, Kazuo, Hirano, Kazuyuki
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Chromatography, Affinity
Chromatography, Gel
Chromatography, Ion Exchange
Chymotrypsin - metabolism
Electrophoresis, Polyacrylamide Gel
Human
Humans
Kallikreins - metabolism
Kinetics
Male
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Peptide Fragments - chemistry
Peptide Mapping
Prostate specific antigen
Prostate-Specific Antigen - isolation & purification
Prostate-Specific Antigen - metabolism
Prostate-Specific Antigen - urine
Protease
Purification
Semen - chemistry
Substrate Specificity
Urine
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Summary:Prostate specific antigen (uPSA) was purified to homogeneity from human urine using SuperQ-Toyopearl, Sulfate-Cellulofine, Phenyl-Toyopearl, CM-Sepharose, anti-urokinase IgG Sepharose and Sephadex G-100. The purified uPSA gave a major band at 32.9 kDa on SDS-PAGE under the reduced condition. However, it shows multiple bands on native PAGE. Substrate specificity of purified uPSA is identical with that of PSA from human seminal plasma and uPSA shows the kallikrein and chymotrypsin-like activities. On the analysis of N-terminal amino acid, two amino acid residues at N-terminal position of uPSA were detected and other amino acid sequence of uPSA was identical with that of sPSA. In addition, we isolated the multiple components of uPSA using anion-exchange chromatography. They were almost the same in amino acid composition and N-terminal amino acid sequences and showed differences in lectin-blotting pattern.
ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/S0304-4165(97)00055-X