Abstract
Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the Vmax of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.
| Original language | English |
|---|---|
| Pages (from-to) | 395-402 |
| Number of pages | 8 |
| Journal | Cellular Signalling |
| Volume | 2 |
| Issue number | 4 |
| State | Published - Dec 1 1990 |
| Externally published | Yes |
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Keywords
- cAMP-dependent
- Mucor rouxii
- Polyamines
- Polycations
- Protein kinase
ASJC Scopus subject areas
- Cell Biology
Cite this
Polyamines and basic proteins stimulate activation by cAMP and catalytic activity of Mucor rouxii cAMP-dependent protein kinase. / Guthmann, Marcelo; Pastori, Ricardo; Moreno, Silvia.
In: Cellular Signalling, Vol. 2, No. 4, 01.12.1990, p. 395-402.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Polyamines and basic proteins stimulate activation by cAMP and catalytic activity of Mucor rouxii cAMP-dependent protein kinase
AU - Guthmann, Marcelo
AU - Pastori, Ricardo
AU - Moreno, Silvia
PY - 1990/12/1
Y1 - 1990/12/1
N2 - Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the Vmax of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.
AB - Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the Vmax of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.
KW - cAMP-dependent
KW - Mucor rouxii
KW - Polyamines
KW - Polycations
KW - Protein kinase
UR - http://www.scopus.com/inward/record.url?scp=0025042902&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025042902&partnerID=8YFLogxK
M3 - Article
C2 - 2174692
AN - SCOPUS:0025042902
VL - 2
SP - 395
EP - 402
JO - Cellular Signalling
JF - Cellular Signalling
SN - 0898-6568
IS - 4
ER -