MG2+ INHIBITS FORMATION OF 4CA2+-CALMODULIN-ENZYME COMPLEX AT LOWER CA2+ CONCENTRATION - H-1 AND CD-113 NMR-STUDIES

被引：0

作者：

OHKI, S

IWAMOTO, U

AIMOTO, S

YAZAWA, M

HIKICHI, K

机构：

[1] HOKKAIDO UNIV,FAC SCI,DEPT POLYMER SCI,SAPPORO,HOKKAIDO 060,JAPAN

[2] HOKKAIDO UNIV,FAC SCI,DEPT CHEM,SAPPORO,HOKKAIDO 060,JAPAN

[3] OSAKA UNIV,INST PROT RES,SUITA,OSAKA 565,JAPAN

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1993年 / 268卷 / 17期

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Our previous H-1 NMR studies indicated that when mastoparan (MP) is added to Ca2+-half-saturated calmodulin (2Ca2+-CaM) in the absence of Mg2+, ions, Ca2+ ions transfer from the C-terminal-half domain of CaM not interacting with MP to the N-terminal-half domain of CaM interacting with MP at lower MP concentrations (Ohki, S., Yazawa, M., Yagi, K., and Hikichi, K. (1991b) J. Biochem. (Tokyo) 110, 737-742). As a consequence, the active form of 4Ca2+-CaM.MP complex is formed. In the present study, we studied the effect of Mg2+ ions on Ca2+ transfer. In the presence of Mg2+ ions, such Ca2+ transfer does not occur. The effects of Mg2+ ions are also studied by observing Cd-113 NMR in the presence of M13, the 26-residue peptide of the CaM-binding region of myosin light chain kinase. The Cd-113 NMR results show that Mg2+ ions prevent to form the active complex. Mg2+ plays an important role as an inactivating factor to CaM.

引用

页码：12388 / 12392

页数：5

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