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Ultracentrifugal Characterization of Pepsin and Pepsinogen

From the ¹ From The Rockefeller University, New York, New York 10021

Chromatographically purified pepsinogen and samples of pepsin freshly prepared from it have been examined in the ultracentrifuge. Sedimentation equilibrium measurements, by the procedure of Yphantis, and sedimentation velocity experiments have been carried out on the zymogen and on the enzyme. Both were found to be homogeneous within the limits of detection of the procedures. The s_20,w of pepsinogen was found to be 3.24 ± 0.15, and that of pepsin, 2.88 ± 0.15 x 10^-13 sec. Values of V were calculated from the amino acid compositions of the two proteins given in the preceding paper (4), and were found to be 0.73₀ ml per g for pepsinogen and 0.72₆ ml per g for pepsin. The molecular weights found were 40,400 ± 1,600 for pepsinogen and 32,700 ± 1,200 for pepsin. These values are in satisfactory agreement with the molecular weights derived from the amino acid compositions.

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