Abstract
Observed changes in the reactivity of the essential sulfhydryl groups of a protein growth factor correlate with changes in its biological activity. In activated and non-activated growth factor, the maximal number of sulfhydryl groups reacting with parachloromercuribenzoate was the same; while the spatial arrangement of the sulfhydryl groups appeared to differ, as evidenced by their different rates of chemical reaction. It is believed that these changes in sulfhydryl reactivity reflect structural changes in the protein molecule and that these structural changes are responsible for the observed changes in its biological activity.
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