funaria hygrometrica/adenosine

The role of purine and pyrimidine ribosides, nucleotides and substituted xanthines in the differentiation of chloronema filaments in suspension cultures of protonema of the moss Funaria hygrometrica Hedw. has been examined. Cyclic adenosine-3',5'-monophosphate (cAMP) and mono-and dibutyryl cAMP

From the protonema of the moss Funaria hygrometrica (L.) Sibth, a factor indistinguishable from cyclic adenosine 3':5'-monophosphate (cAMP) has been isolated. The factor stimulated the activity of protein kinase from rabbit skeletal muscle and co-chromatographed with authentic cAMP in two solvent

Suspension cultures of intact chloronema cells of the moss Funaria hygrometrica take up [(3)H]cAMP and degrade it rapidly. The increase in total radioactivity accumulated by the cells was linear up to 30 minutes. Initially, the major degradation products were 5'-AMP and adenosine, but later

Soluble proteins extracted with Tris-buffer pH 8.8 from both differentiation stages of the protonema of Funaria hygrometrica (chloronema and caulonema) were separated by microgel electrophoresis. 4x10(-3) mg protein/gel was applied. The caulonema, which is the only part of the protonema able to form