Immunochemical studies on the specificity of the peanut ( Arachis hypogaea) Agglutinin

• Published in: Carbohydrate research 1976-10, Vol.51 (1), p.107-118
• Main Authors: E.A. Pereira, Miercio, Kabat, Elvin A., Lotan, Reuben, Sharon, Nathan
• Format: Article
• Language: English
• Subjects: Animals; Arachis; Binding Sites, Antibody; Blood Group Antigens; Cattle; Female; field crops; Gastric Mucosa; Hemagglutination Tests; Humans; Kinetics; Lectins; Monosaccharides; Oligosaccharides; Ovarian Cysts; plant biochemistry; Plant Lectins; plant physiology; Precipitin Tests; Saliva; Swine
• ISSN: 0008-6215; 1873-426X
• DOI: 10.1016/S0008-6215(00)84040-9

The specificity of purified, peanut agglutinin has been studied immunochemically by quantitative precipitin and inhibition assays. The lectin showed substantial differences in precipitating with blood-group substances of the same specificity. Of the B substances tested, horse 4 25% completely precipitated the lectin, Beach phenol insoluble failed to interact, and PM phenol insoluble gave an intermediate reaction. The lectin did not precipitate with A 1 substances, with hog gastric mucin A + H substance, or with A 2 substance WG phenol insoluble. Another A 2 substance, cyst 14 phenol insoluble, precipitated ∼2/3 of the lectin. Of the H substances, Tighe phenol insoluble was inactive, JS phenol insoluble precipitated poorly, and Morgan standard H precipitated about 80% of the lectin. However, first stage of Smith degradation, as well as Pl fractions obtained by mild acid hydrolysis of blood-group substances, gave products which precipitated strongly. The lectin was also completely precipitated by all precursor blood-group substances, as well as by cows 21 and 26, all having strong I-Ma, I-Ort, I-Step, and I-Da activities. Cow 18, which does not possess significant blood-group I activity, precipitated very slightly. Fractions of blood-group substances N-1(Le a)and Tij (B) obtained by precipitation from 90 percent phenol at higher concentrations of ethanol interacted better with peanut agglutinin. These differences in activity are ascribable to a heterogeneity resulting from incomplete biosynthesis of carbohydrate side-chains of blood-group substances, particularly resulting in variations in the numbers of dGalβ1 → 3 dGalNAC or dGalβ1→ 4 dGlcNAc determinants. The agglutinin reacted with the hydatid cyst P 1 glycoprotein, as well as with the previously studied antifreeze and sialic acid-free α1 acid glycoproteins, but not with pneumococcus type XIV polysaccharide. Inhibition of precipitation showed the lectin to be most specific for the disaccharide dGalβ1 → 3 dGalNac, which is 14, 55, and 90 times as active as dGalβ1 → 4 dGlcNac, dGal, and dGalβ1 → 3 dGlcNac, respectively. dGalβ1 → 3 N-