A cyclic AMP-independent protein kinase from <i>Candida albicans</i>

Roy, B.Gupta; Datta, Asis

doi:10.1042/bj2340543

Cited by 3 publications

(1 citation statement)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Like a protein kinase of Candidu albicans, Legionella micdadei PK I was markedly inhibited by the polyamines spermine and spermidine (Gupta Roy & Datta, 1986).…”

Section: Discussionmentioning

confidence: 99%

Demonstration of Two Protein Kinases in Extracts of Legionella micdadei

Saha

Dowling²,

Mukhopadhyay³

et al. 1988

Microbiology

View full text Add to dashboard Cite

Protein kinases I (PK I) and I1 (PK 11) were purified 253-and 13.5-fold, respectively, from an extract of sonically disrupted cells of Legionella micdadei by ion-exchange chromatography on QAE-Sephadex, by histone affinity chromatography, and by HPLC-gel filtration chromatography. Both enzymes catalysed the phosphorylation of calf thymus histones, with a K , of 2.7mgml-I for PK I and 2.9 mg ml-l for PK 11. Histone HZb was the best protein kinase substrate for both PK I and PK 11. The pH optima were 6.8 and 7.0 for PK I and PK I1 respectively. The K , for ATP was 0-29 mM for PK I and 0.33 mM for PK 11. PK I1 activity was stimulated by either CAMP or cGMP, whereas PK I was inhibited by both cyclic nucleotides. The activity of PK I was unaffected by addition of calmodulin, diacylglycerol and mixtures of Ca2+ and acidic phospholipids, but these additions increased PK I1 activity threefold. The activity of PK I1 was stimulated by spermine and spermidine, but PK I was inhibited by these compounds. PK I and PK I1 were both strongly inhibited by heparin.

show abstract

“…Like a protein kinase of Candidu albicans, Legionella micdadei PK I was markedly inhibited by the polyamines spermine and spermidine (Gupta Roy & Datta, 1986).…”

Section: Discussionmentioning

confidence: 99%