guanidine/karvane sojauba

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Quantitative Measurement of the Ability of Different Mutagens to Induce an Inherited Change in Phenotype to Allow Maltose Utilization in Suspension Cultures of the Soybean, GLYCINE MAX (L.) Merr.

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USING A NEWLY DEVELOPED PLATING SYSTEM, WE HAVE MEASURED CELL SURVIVAL AND THE FREQUENCIES OF VARIATION IN AN INHERITED TRAIT AFTER TREATMENT OF SOYBEAN CELL SUSPENSIONS WITH DIFFERENT MUTAGENS: ethyl methanesulfonate (EMS), methyl methanesulfonate (MMS), N-Methyl-N'-nitro-N-nitroso-guanidine

Role of intramolecular high-mannose chains in the folding and assembly of soybean (Glycine max) lectin polypeptides: studies by the combined use of spectroscopy and gel-filtration size analysis.

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It was previously reported [Nagai, K. & Yamaguchi, H. (1993) J. Biochem. 113, 123-125] that intramolecular high-mannose chains are essential for reconstitution of soybean lectin from denatured subunits. To obtain more detailed information on the role of the intramolecular high-mannose chains in the

Direct demonstration of the essential role of the intramolecular high-mannose oligosaccharide chains in the folding and assembly of soybean (glycine max) lectin polypeptides.

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We investigated the role of the intramolecular high-mannose oligosaccharide chains in the folding and assembly of soybean lectin polypeptides. Soybean lectin, dissociated into subunits and completely denatured in 6 M guanidine hydrochloride, was quantitatively reconstituted to the active tetrameric

Soybean hydrophobic protein. Isolation, partial characterization and the complete primary structure.

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A 9000-Mr protein isolated from a 60% ethanolic extract of soybean (Glycine max) seeds has been characterized and fully sequenced. The protein consists of 80 amino acid residues with four disulfide bonds. It contains a large number of hydrophobic residues and lacks methionine, phenylalanine,

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