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ISOLATION OF A LOW MOLECULAR WEIGHT GLYCOPROTEIN IN THE HUMAN URINE: COMPARISON WITH URINARY PEMPHIGOID ANTIGEN
Author(s) -
Miyagawa Sachiko,
Yonemasu Kunio,
Okuchi Toshie,
Sakamoto Kuniki
Publication year - 1984
Publication title -
the journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.9
H-Index - 65
eISSN - 1346-8138
pISSN - 0385-2407
DOI - 10.1111/j.1346-8138.1984.tb01506.x
Subject(s) - glycoprotein , urine , chemistry , polyacrylamide gel electrophoresis , size exclusion chromatography , antigen , chromatography , ultrafiltration (renal) , gel electrophoresis , cicatricial pemphigoid , biochemistry , microbiology and biotechnology , antibody , bullous pemphigoid , biology , immunology , pemphigoid , enzyme
A glycoprotein was isolated from the urine of normal individuals and patients with bullous pemphigoid by means of ultrafiltration, ion exchange chromatography, and gel filtration. The yield of the purified glycoprotein from each liter of pooled urine was 0.35–0.40 mg. Analysis of the glycoprotein on SDS‐polyacrylamide gel electrophoresis showed a single band of approximate molecular weight 23 kd. The glycoprotein contained approximately 2.5% (w/w) carbohydrate. The glycoprotein differed from the urinary pemphigoid antigen described by Diaz et al (1), though both were nondialyzable, cathodally migrating, low molecular weight glycoproteins in the human urine. The significance of the glycoprotein is unclear at present, but it might be useful for studies of the metabolic degradation process of serum proteins.