The isolation of two proteins, glycoprotein I and a trypsin inhibitor, from the seeds of kidney bean (Phaseolus vulgaris).

1. The isolation of two proteins from the seeds of kidney bean is described. 2. The individual steps in the purification procedure included: extraction of the seeds at pH9.0, dialysis, first against pH9.0 and then against pH5.0 buffers, high-voltage electrophoresis of the proteins soluble at pH5.0 and chromatography on Sephadex G-200, Sephadex G-75 and DEAE-Sephadex columns. 3. Of the two proteins isolated, the first and larger component was a glycoprotein and its carbohydrate part was mainly composed of d-mannose and d-glucosamine together with smaller amounts of arabinose, xylose and fucose. 4. The second protein component isolated was a trypsin inhibitor and was almost entirely devoid of sugars but contained a firmly bound pinkish-blue pigment. 5. The amino acid composition of the two proteins was determined. 6. The glycoprotein contained very little if any cyst(e)ine but was relatively rich in aromatic amino acids, whereas the trypsin inhibitor had an unusually high cystine content (nearly 15%) but was relatively poor in valine and in aromatic amino acids.