ISSN:
0739-4462
Keywords:
cyclic AMP
;
protein phosphorylation
;
subcellular fractionation
;
tick salivary glands
;
Chemistry
;
Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
Notes:
Phosphoproteins were examined by electrophoresis and autoradiography in fractions of tick salivary glands. When whole salivary glands were preincubated in 32Pi, then stimulated by 10 μM dopamine and subsequently fractionated, substantial phosphate was incorporated into 45,000-, 47,000-, and 62,000-dalton proteins of the plasma membrane-rich 11,500g pellet and 100,000g supernatant. When tissue homogenates were incubated in [γ-32P] ATP prior to subcellular fractionation, the 62,000-, 47,000-, and 45,000-dalton proteins were enhanced by cyclic AMP in all fractions and were most prominent in the membrane-rich 11,500g fraction. Phosphoproteins of the same molecular masses were also found in the 11,500g pellet and 100,000g supernatant when labelled with [γ-32P] ATP in the presence of cAMP.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/arch.940050104
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