Hemagglutinating activity of proteins from Parkia speciosa seeds.
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 mug/muL. 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 mug/muL. 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).
Chankhamjon
Kanokwan
K
Research Center for Bioorganic Chemistry, Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok, Thailand.
Petsom
Amorn
A
Sawasdipuksa
Narumon
N
Sangvanich
Polkit
P
D000818:Animals; D004912:Erythrocytes / Q000187:drug effects / Q000502:physiology; D007887:Fabaceae; D006041:Goats; D006384:Hemagglutination / Q000187:drug effects* / Q000502:physiology; D010936:Plant Extracts / Q000302:isolation & purification* / Q000494:pharmacology; D010940:Plant Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D011817:Rabbits; D012639:Seeds; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods
D010936:Plant Extracts; D010940:Plant Proteins