Hemagglutinating activity of proteins from Parkia speciosa seeds

Abstract

Proteins from Parkia speciosa Hassk. (Fabaceae) seeds were extracted and stepwise precipitated using ammonium sulfate. Proteins precipitated with 25% ammonium sulfate were separated by affinity chromatography on Affi-Gel Blue gel followed by protein liquid chromatography on Superdex 200. The protein Gj, which was identified as a protein similar to putative aristolochene synthase, 3′-partial from Oryza sativa L. (Poaceae), had hemagglutinating activity of 0.39 μg/μL. Moreover, fraction C2 from the proteins precipitated with 60% ammonium sulfate, separated by lectin-specific adsorption chromatography using Con A Sepharose, had hemagglutinating activity of 1.17 μg/μL. Using gel electrophoresis, two proteins C2a and C2b were separated, having molecular weights of 45 kDa and 23 kDa, respectively. From protein identification, C2a was found to be similar to the hypothetical protein B1342F01.11 from Oryza sativa, and C2b was similar to the hypothetical protein At1g51560 from Arabidopsis thaliana (L.) Heynh. (Brassicaceae).

Keywords::

• Parkia speciosa
• seed proteins
• hemagglutinating
• affinity chromatography

Declaration of interest: We thank the Thailand Research Foundation for financial support and Chulalongkorn University for a Graduate Scholarship. The authors alone are responsible for the writing of this paper.