Abstract
Crystalline Fraction I protein from tobacco has been dissociated and separated into three large subunit polypeptides and two small subunit polypeptides by isoelectric focusing in polyacrylamide gels containing 8 m urea. The three large subunit polypeptides, resolved by isoelectric focusing, could not be differentiated by amino acid analysis or by fingerprinting of trypsin or chymotrypsin hydrolysates of the individual polypeptides. The two small subunit polypeptides, resolved by hydroxylapatite chromatography in 0.1% sodium dodecyl sulfate as well as by isoelectric focusing, were shown to be distinct polypeptides. The two polypeptides were shown to have different tyrosine:tryptophan ratios, shown by ultraviolet spectra in 0.1 m NaOH, and different tyrosine contents shown by amino acid analysis, and they gave different peptide fingerprints after trypsin hydrolysis. The two small subunit polypeptides are concluded to be separate gene products but the three large subunit polypeptides are believed to be the result of modification of a single gene product.
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