Incidence of a split alpha 2-glycoprotein band in the electrophoretic pattern for serum of adenocarcinoma patients

• Published in: Clinical chemistry (Baltimore, Md.) Vol. 26; no. 3; p. 392
• Main Authors: Dermer, G B, Silverman, L M, Gendler, S J, Tökés, Z A
• Format: Journal Article
• Language: English
• Published: England 01-03-1980
• Subjects: Adenoma - blood; alpha-Macroglobulins - analysis; Electrophoresis, Cellulose Acetate; Electrophoresis, Polyacrylamide Gel; Female; Humans; Leukemia - blood; Lymphoma - blood; Male; Molecular Weight; Neoplasms - blood
• ISSN: 0009-9147
• DOI: 10.1093/clinchem/26.3.0392

We electrophoresed serum samples on Mylar-backed cellulose acetate membranes and stained for glycoproteins with the periodic acid--Schiff reagent. The samples were from untreated adenocarcinoma patients, adenocarcinoma patients receiving chemotherapy, and patients with other malignancies, and also from patients with benign proliferative diseases, inflammatory diseases, and other non-malignant conditions. Forty-five per cent of the sera from untreated adenocarcinoma patients and 80% of those from adenocarcinoma patients with progressive systemic disease exhibited a splitting of the alpha 2-glycoproteins into a fast and slow band. Such a pattern was seen in only 4% of the non-adenocarcinoma cancer patients and 4% of the control group. Serial studies indicated that electrophoretic patterns of alpha 2-glycoproteins change with clinical status. Non-cancer patients with high concentrations of acute-phase proteins in their serum did not exhibit two alpha 2-glycoprotein bands. Further characterization of serum proteins from the fast alpha 2 region suggest that alpha 1-acid glycoprotein and haptoglobin beta chains are the principal components staining with periodic acid--Schiff reagent. These components are markedly less apparent in, or are absent from, the fast alpha 2 region of normal sera.