CALCYCLIN FROM MOUSE EHRLICH ASCITES TUMOR-CELLS AND RABBIT LUNG FORM NONCOVALENT DIMERS

被引:19
作者
WOJDA, U [1 ]
KUZNICKI, J [1 ]
机构
[1] M NENCKI INST EXPTL BIOL, PL-02093 WARSAW, POLAND
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1994年 / 1209卷 / 02期
关键词
CALCIUM BINDING PROTEIN; S100; PROTEIN; CALCYCLIN; DIMERIZATION; COVALENT AND NONCOVALENT DIMER;
D O I
10.1016/0167-4838(94)90192-9
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
Crosslinking treatments of fresh cytosol from mouse Ehrlich ascites tumor (EAT) cells revealed the existence of calcyclin dimers which were sensitive to SDS, but not to reducing agents, which suggests the existence of non-covalent dimers. In stored EAT cell cytosol and preparations of purified calcyclin dimers were also formed by S-S bridging (covalent dimers). The S-S dimers did not bind to organomercurial Agarose and could be separated from reduced forms of calcyclin that bound to the resin. Calcyclin eluted from the resin with DTT was a mixture of monomers and non-covalent dimers as shown by crosslinking and subsequent immunoblotting. Calcyclin from rabbit lung, lacking a cysteine residue, could also be crosslinked as a dimer. It is suggested that the ability of calcyclin to form non-covalent dimers is of physiological significance.
引用
收藏
页码:248 / 252
页数:5
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