Isolation of concanavalin a binding protein(s) from rat erythrocyte stroma

• Published in: Biochimica et biophysica acta Vol. 271; no. 2; pp. 378 - 387
• Main Authors: Akedo, Hitoshi, Mori, Yoichi, Tanigaki, Yumiko, Shinkai, Kiyoko, Morita, Kazuko
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 21.07.1972
• Subjects: Amino Acids - analysis; Ammonium Sulfate; Animals; Chemical Precipitation; Chromatography, Gel; Concanavalin A - analysis; Concanavalin A - isolation & purification; Crystallization; DNA - biosynthesis; Electrophoresis, Disc; Erythrocytes - analysis; Glycoproteins - analysis; Glycoproteins - blood; Glycoproteins - isolation & purification; Hexoses - analysis; Isoelectric Focusing; Lectins; Lymphocyte Activation; Lymphocytes - metabolism; Molecular Weight; Neuraminic Acids - analysis; Protein Binding; Rats; Sodium Dodecyl Sulfate; Thymidine - metabolism; Tritium; Ultracentrifugation
• ISSN: 0005-2795; 0006-3002; 1879-2952; 1878-2434
• DOI: 10.1016/0005-2795(72)90213-9

Concanavalin A was purified and crystallized from Canavalia gladiata. The crystallized concanavalin A possessed properties similar in biological respects to those from Canavalia ensiformis. However, their physicochemical properties differed slightly from each other. Concanavalin A from Canavalia gladiata agglutinates various types of animal cells and stimulates blast formation of human and rat peripheral lymphocytes. On isoelectric focusing in polyacrylamide gel concanavalin A was separated into eight protein bands. From rat erythrocyte stroma two glycoproteins which were agglutinated by concanavalin A were isolated and purified. The molecular weights of these proteins were estimated as 2 · 10 5 and 3 · 10 5, respectively. Both of the glycoproteins contained a relatively large amount of hexose and a small quantity of sialic acid. No hexosamine was detected.