Sedimentability of microsomal nucleoprotein from rat liver homogenates in ionic media I. Precipitation of pentose nucleoprotein by cacl2.
✍ Scribed by Gross, Paul R. ;Pearl, William
- Book ID
- 102878007
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1958
- Tongue
- English
- Weight
- 864 KB
- Volume
- 52
- Category
- Article
- ISSN
- 0095-9898
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✦ Synopsis
Y o r k CLty FIVE FlGURES
Recently, Swedish (Hultin, '50a, '50b) and American (Gross, '54, '56) workers have shown that the addition of CaC1, in low concentrations to sea urchin egg liornogenates initiates a series of reactions paralleling very closely those which, in zlico, accompany fertilization, sol-gel transformations, and the so-called "surface precipitation reaction" of injury (Heilbrunn, '52). Among these reactions is an aggregation process involving macromolecular materials and evidenced by greatly enhanced sedimentability of protein and pentosenucleic acid from the homogenates. I n a previous publication, one of us (Gross, '56) has discussed evidence that the aggregating fraction is a nucleoprotein particle whose physical properties place it among the PNA-rich particulates of the microsome fraction. It has been suggested that this Ca-initiated reaction sequence, culminating in viscosity increase, acid formation, increased Qo0, and lysis of certain cytoplasmic inclusions, is either identical with o r related t o the normal sol-gel transformation mechanism in z-ivo.
'Aided by a grant from the American Cancer Society. a Some of the data rrported here have been the subject of preliminary notes: