Phosphorylation of the purified CaCB-receptor.
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Phosphorylation of the purified CaCB-receptor. / Röhrkasten, A; Nastainczyk, W; Sieber, M; Jahn, Holger; Regulla, S; Hofmann, F.
in: J CARDIOVASC PHARM, Jahrgang 12, Nr. 5, 5, 1988, S. 43-46.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Phosphorylation of the purified CaCB-receptor.
AU - Röhrkasten, A
AU - Nastainczyk, W
AU - Sieber, M
AU - Jahn, Holger
AU - Regulla, S
AU - Hofmann, F
PY - 1988
Y1 - 1988
N2 - The purified receptor for calcium channel blockers (CaCB-receptor) from rabbit skeletal muscle contains three polypeptides within a molecular mass of 165, 55, and 32 kDa. cAMP-dependent protein kinase was shown to phosphorylate preferentially the 165-kDa protein. The major phosphorylation site was identified and compared with the recently published primary sequence of the CaCB-receptor. It is concluded that serine 687 is the phosphorylation site. Phosphorylation of serine 687 may regulate the open-state probability of the CaCB-receptor.
AB - The purified receptor for calcium channel blockers (CaCB-receptor) from rabbit skeletal muscle contains three polypeptides within a molecular mass of 165, 55, and 32 kDa. cAMP-dependent protein kinase was shown to phosphorylate preferentially the 165-kDa protein. The major phosphorylation site was identified and compared with the recently published primary sequence of the CaCB-receptor. It is concluded that serine 687 is the phosphorylation site. Phosphorylation of serine 687 may regulate the open-state probability of the CaCB-receptor.
M3 - SCORING: Zeitschriftenaufsatz
VL - 12
SP - 43
EP - 46
JO - J CARDIOVASC PHARM
JF - J CARDIOVASC PHARM
SN - 0160-2446
IS - 5
M1 - 5
ER -