Purification and characterization of a calcium-dependent protein kinase from beetroot plasma membranes
✍ Scribed by Bárbara Lino; M. Teresa Carrillo-Rayas; Alicia Chagolla; Luis E. González de la Vara
- Publisher
- Springer-Verlag
- Year
- 2006
- Tongue
- English
- Weight
- 348 KB
- Volume
- 225
- Category
- Article
- ISSN
- 0032-0935
No coin nor oath required. For personal study only.
📜 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
Roots of many species respond to gravity (gravitropism) and grow downward only if illuminated. This light-regulated root gravitropism is phytochromedependent, mediated by calcium, and inhibited by KN-93, a specific inhibitor of calcium/calmodulin-dependent protein kinase II (CaMK II). A cDNA encodin
Membranes isolated from pea buds contain protein-kinase activity which is greatly activated by low concentrations of calcium ions. This paper describes a simple purification of this enzyme with a novel means of detecting enzyme activity by Western blotting. The purified enzyme appears to autophospho