Abstract
Gel electrophoresis and sucrose density gradient centrifugation techniques permitted the visualization for the first time of the ternary complex formed by the binding of cAMP to Mucor rouxii cAMP-dependent protein kinase holoenzyme. The addition of 0.5 M NaCl or histone plus ATP-Mg++, together with cAMP, dissociates the holoenzyme into free regulatory (R) and catalytic (C) subunits. At 4°C, cAMP bound to the holoenzyme is readily exchangeable with unlabeled cAMP (half life 2.5 min), while the nucleotide bound to the R subunit has a very slow exchange rate (half life 210 min). The amount of cAMP bound to R subunit is approximately twice the amount bound to holoenzyme at saturation.
| Original language | English |
|---|---|
| Pages (from-to) | 663-671 |
| Number of pages | 9 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 101 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jul 30 1981 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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cAMP-dependent protein kinase from Mucor rouxii : Physical evidence of a ternary complex holoenzyme-cAMP. / Pastori, Ricardo; Kerner, N.; Moreno, S.; Passeron, S.
In: Biochemical and Biophysical Research Communications, Vol. 101, No. 2, 30.07.1981, p. 663-671.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - cAMP-dependent protein kinase from Mucor rouxii
T2 - Physical evidence of a ternary complex holoenzyme-cAMP
AU - Pastori, Ricardo
AU - Kerner, N.
AU - Moreno, S.
AU - Passeron, S.
PY - 1981/7/30
Y1 - 1981/7/30
N2 - Gel electrophoresis and sucrose density gradient centrifugation techniques permitted the visualization for the first time of the ternary complex formed by the binding of cAMP to Mucor rouxii cAMP-dependent protein kinase holoenzyme. The addition of 0.5 M NaCl or histone plus ATP-Mg++, together with cAMP, dissociates the holoenzyme into free regulatory (R) and catalytic (C) subunits. At 4°C, cAMP bound to the holoenzyme is readily exchangeable with unlabeled cAMP (half life 2.5 min), while the nucleotide bound to the R subunit has a very slow exchange rate (half life 210 min). The amount of cAMP bound to R subunit is approximately twice the amount bound to holoenzyme at saturation.
AB - Gel electrophoresis and sucrose density gradient centrifugation techniques permitted the visualization for the first time of the ternary complex formed by the binding of cAMP to Mucor rouxii cAMP-dependent protein kinase holoenzyme. The addition of 0.5 M NaCl or histone plus ATP-Mg++, together with cAMP, dissociates the holoenzyme into free regulatory (R) and catalytic (C) subunits. At 4°C, cAMP bound to the holoenzyme is readily exchangeable with unlabeled cAMP (half life 2.5 min), while the nucleotide bound to the R subunit has a very slow exchange rate (half life 210 min). The amount of cAMP bound to R subunit is approximately twice the amount bound to holoenzyme at saturation.
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UR - http://www.scopus.com/inward/citedby.url?scp=0019891331&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(81)91310-3
DO - 10.1016/0006-291X(81)91310-3
M3 - Article
C2 - 6272765
AN - SCOPUS:0019891331
VL - 101
SP - 663
EP - 671
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -