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A Ribonucleoprotein Which Catalyzes Thiol-Disulfide Exchange in the Sea Urchin Egg

From the ¹ From the Department of Biochemistry, College of Physicians and Surgeons, Columbia University, New York, New York 10032

Some properties of a ribonucleoprotein which catalyzes electron exchange between the disulfide groups of the contractile protein of the cell cortex and the sulfhydryl groups of a protein from the mitotic apparatus are described.

The enzyme was purified 400-fold by molecular sieve chromatography. The purified enzyme contains about 20% ribonucleic acid with a ratio of guanylic plus cytidylic acid to adenylic plus uridylic acid about 1.3. The nucleotide moiety is resistant to ribonuclease but is cleaved by venom phosphodiesterase. The s_20,w of the whole ribonucleoprotein is 1.42 with a molecular weight of 13,500. Three sulfhydryl groups were detected in the enzyme.

Separation of the enzyme into the protein and nucleic acid components results in complete loss of catalytic activity, which is largely restored on recombination.

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