Electrophoretic studies on the plasma proteins of patients with neoplastic disease. II. An acid protein present in the plasma

✍ Scribed by Mary L. Petermann; Katharine R. Hogness

• Publisher: John Wiley and Sons
• Year: 1948
• Tongue: English
• Weight: 392 KB
• Volume: 1
• Category: Article
• ISSN: 0008-543X
• DOI: 10.1002/1097-0142(194805)1:1<104::aid-cncr2820010108>3.0.co;2-n

✦ Synopsis

W HEN the plasma proteins of patients with gastric cancer are analyzed electrophoretically in alkaline solution, some of the components are found to be present in abnormal amounts.12 The decrease in albumin and increases in a-globulins and fibrinogen are similar to those found in many wasting diseases, however, and no abnormality characteristic of cancer can be discerned. The possibility exists, nevertheless, that in othjer buffers and at different hydrogen ion concentrations, electrophoretic analysis may reveal the presence of some specific change in the plasmaprotein patterns of patients with cancer. Since it was found by Luetscher that purified human serum albumin separates into two components at pH 4.0 in acetate buffer, the same pH was chosen for the experiments described in this report.

At pH 4.0 in an acetate-chloride buffer, the plasma albumin and most of the other proteins carry a positive net charge and migrate toward the cathode. In most samples of plasma another small boundary is also seen that moves in the opposite direction; this indicates the presence of a substance that is negatively charged at pH 4.0 and therefore has an isoelectric point much lower than those of the well-known plasma proteins.