Nippostrongylus brasiliensis: occurrence of multiple protein kinases.
The presence of cyclic AMP-dependent protein kinase and phosvitin kinases, with activity independent of cyclic nucleotides, was shown in the intestinal nematode Nippostrongylus brasiliensis. The activity of the cyclic AMP-dependent protein kinase was found to be enhanced about 8-fold in the presence of 10(-7) M cyclic AMP; the apparent Km values were determined to be 20 microM and 80 microM for ATP and kemptide, respectively. The molecular weight of the holoenzyme was about 170 000. Two phosvitin kinases could be isolated and distinguished by their molecular weights of 600 000 and 40 000. The activity of the high-molecular-weight phosvitin kinase was effectively inhibited by suramin and heparin. The apparent Km values were found to be 30 microM and 0.1 mg/ml for ATP and phosvitin, respectively. In the case of the low-molecular-weight phosvitin kinase the apparent Km values for ATP and phosvitin were found to be 30 microM and 0.6 mg/ml, respectively. The investigation of different developmental stages of N. brasiliensis revealed a marked higher level of protein kinase activity in the L4 larvae compared to L3 larvae and adults.
D000818:Animals; D006493:Heparin / Q000494:pharmacology; D006657:Histones / Q000378:metabolism; D007814:Larva / Q000201:enzymology; D009559:Nippostrongylus / Q000201:enzymology*; D009842:Oligopeptides / Q000378:metabolism; D010774:Phosvitin / Q000378:metabolism; D011494:Protein Kinases / Q000032:analysis* / Q000378:metabolism; D051381:Rats / Q000469:parasitology; D013379:Substrate Specificity; D013498:Suramin / Q000494:pharmacology
D006657:Histones; D009842:Oligopeptides; D013498:Suramin; C037642:kemptide; D006493:Heparin; D010774:Phosvitin; D011494:Protein Kinases