Purification and Characterization of Human Sarcomeric Mitochondrial Creatine Kinase
✍ Scribed by Ursula Walterscheid-Müller; Siegmund Braun; Willi Salvenmoser; Georg Meffert; Otto Dapunt; Erich Gnaiger; Stephan Zierz; Raimund Margreiter; Markus Wyss
- Book ID
- 115632363
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 684 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0022-2828
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Mitochondrial creatine kinase (MtCK) plays a central role in energy homeostasis within cells that display high and variable rates of ATP turnover. Vertebrate MtCKs exist primarily as octamers but readily dissociate into constituent dimers under a variety of circumstances. MtCK is an ancient protein
Creatine kinase (CK), catalyzing the reversible trans-phosphorylation between ATP and creatine, plays a key role in the energy metabolism of cells with high and fluctuating energy requirements. We have solved the X-ray structure of octameric human ubiquitous mitochondrial CK (uMtCK) at 2.7 Å resolut