Purification and characterization of cytoplasmic creatine kinase isozymes ofXenopus laevis
β Scribed by J. Robert; H. R. Kobel
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 671 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0006-2928
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π SIMILAR VOLUMES
A calcium-sensitive, phospholipid-dependent protein kinase (protein kinase C) and its three isozymes were purified from rat heart cytosolic fractions utilizing a rapid purification method. The purified protein kinase C enzyme showed a single polypeptide band of 80 KDa on SDS-polyacrylamide gel elect
The enzyme N-acetyl-0-D-glucosaminidase was purified from the cortical granules of Xenopus laevis eggs using affinity chromatography, gel filtration, and density gradient centrifugation. The enzyme had a molecular weight of 37,000-40,000 as determined by polyacrylamide gel electrophoresis and densit
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