Purification and properties of transcription factor IIIA (TF IIIA) from maize pollen (Zea mays L.) are presented for the first time. The purified protein has a molecular mass of about 35 kDa and exibits binding affinity toward both 5S rRNA and 5S rRNA gene. It also facilitates transcription of the 5S rRNA gene in a HeLa cell extract.
The lectin isolated from the leaves of Iris hybrida binds specifically N-acetyl-galactosamine and lactose. Its molecule consists of two identical subunits bound by disulfide bonds. The lectin is a glycoprotein containing about 12% of sugars. It binds asialoglycoproteins containing complex type sugar chains. The binding is reduced by half at the concentration of 0.15 to 0.40 mM of the galactose containing disaccharides irrespectively to a type of galactose isomer. This indicates rather broad specificity of I. hybrida leaf lectin.
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