Isolation and physicochcmical characterization of a lectin from Egyptian Lens culinaris seeds [electronic resource].
فصل ودراسة الخواص الفيزيوكيميائية للكتين المفصول من بذور العدس المصرى.
- p.1601-1614.
Includes references.
A plant lectin has been isolated in pure state from the Egyptian seeds of Lens' culinaris (LCL). The purified lectin showed two protein bands (6372 and 18968 Da). It agglutinated human, rabbits and rats erythrocytes but weakly agglutinated chicken erythrocytes, while no agglutination occurred with sheep erythrocytes. Of the various sugars tested, LCL. agglutination was best inhibited by mannose. Analysis of amino acids composition revealed that LCL was rich in acidic and hydroxy amino acids while totally lacking sulfur amino acids. The lectin was a glycoprotein with 3 % carbohydrate and required divalent metal cations calcium and manganese for full activity. The pH gradient test showed that it was acidic pH sensitive. Thermal denaturation profile demonstrated that it remained fairly stable below 60°C for 30 min.