ISSN:
0148-7280
Keywords:
cAMP-binding protein
;
cAMP-dependent protein kinase
;
sea urchin
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
Notes:
In the sea urchin, Strongylocentrotus intermedius, cAMP-binding capacity was found in the sedimentable fractions obtained by centrifuging the homogenate of the embryos at 10,000g for 20 min and 105,000g for 1 h, and also the supernatant fraction by centrifugation at 105,000g. The cAMP-binding capacity was estimated depending on the radioactivity of 3H-cAMP found in the nonfiltered matter obtained by a filtration through a Millipore filter of a mixture containing 3H-cAMP and each fraction. Prior to the filtration, the mixture was incubated at 0°C for 1 hr. In all fractions, the addition of nonlabeled cAMP to the mixture containing 3H-cAMP resulted in a marked decrease in the radioactivity in the nonfiltered matter. cGMP, cTMP, and cUMP caused only a slight decrease in the radioactivity in the nonfiltered matter. These indicate that specific cAMP binding occurs in the nonfiltered matter of all fractions. The extent of decrease in 3H-radioactivity by cIMP was higher than that caused by cAMP in the 10,000g sedimentable fraction, but in the other fractions, it was as low as observed when cGMP, cTMP, and cUMP were added. This suggests that the nature of cAMP-binding matter in this fraction differs somewhat from those in the other fractions. cAMP-binding capacity in this fraction (10,000g sedimentable fraction) increased gradually during development and the capacity in the other fractions, especially in the supernatant fraction, decreased at the gastrula stage. Protein kinase activity was also found in these fractions. Alteration of intracellular distribution of cAMP-binding proteins and protein kinases during development probably shows the change in the role of protein kinase in the mechanism of development.
Additional Material:
2 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/mrd.1120060104
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