Abstract
Proteins diffusing from tobacco pollen grains exhibit different phosphohydrolytic activities. Molecular sieving produces nuclease fractionation into forms I, II and III with apparent molecular masses ≥ 60 × 103, 32.9 × 103 and 24.6 × 103, respectively, and separation of principal forms II and III from phosphatase and major part of 5′- and 3′-nucleotidase activities. These forms did not differ in the mode of substrate attack and were combined for further enzyme characterization.
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