American Society of Hematology

Fig. 2.

$Fig. 2. Peptidylprolyl cis-trans isomerase activity displayed by fractions from the Sephacryl S-300 gel-filtration column. Aliquots of 100 μL each (from 1.8-mL fractions) were examined, without alteration, for peptidylprolyl cis-trans isomerase activity using Suc-Ala-Leu-Pro-Phe-p-nitroanilide as the substrate, as described previously.40 Standards used for calibrating the gel-filtration column were thyroglobulin, 669 kD; apoferritin, 443 kD; β-amylase, 200 kD; and yeast alcohol dehydrogenase, 150 kD. The peak at fraction no. 42 corresponds to a mass of approximately 490 kD. The peak at fraction no. 51 corresponds to a mass of approximately 280 kD.$

Peptidylprolyl cis-trans isomerase activity displayed by fractions from the Sephacryl S-300 gel-filtration column. Aliquots of 100 μL each (from 1.8-mL fractions) were examined, without alteration, for peptidylprolyl cis-trans isomerase activity using Suc-Ala-Leu-Pro-Phe-p-nitroanilide as the substrate, as described previously.40 Standards used for calibrating the gel-filtration column were thyroglobulin, 669 kD; apoferritin, 443 kD; β-amylase, 200 kD; and yeast alcohol dehydrogenase, 150 kD. The peak at fraction no. 42 corresponds to a mass of approximately 490 kD. The peak at fraction no. 51 corresponds to a mass of approximately 280 kD.

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