✦ LIBER ✦

Separation of calmodulin from calcium-activated protein kinase using calcium-dependent hydrophobic interaction chromatography

✍ Scribed by N.H. Battey; M.A. Venis

Publisher: Elsevier Science
Year: 1988
Tongue: English
Weight: 1020 KB
Volume: 170
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(88)90097-8

No coin nor oath required. For personal study only.

✦ Synopsis

To determine whether a Ca2+-activated protein kinase is regulated by calmodulin, it is necessary to separate it from endogenous calmodulin and from protein kinase activity that is not calcium dependent. We describe here a procedure for achieving these goals using Ca2+-dependent hydrophobic interaction chromatography on phenyl Sepharose in combination with a pH change. The procedure is based on the observation that while calmodulin solubilized from apple fruit membranes binds to phenyl Sepharose in a Ca2+-dependent fashion at both pH 7.0 and 8.5, Ca2+-activated protein kinase from the same source only shows a Ca2+-dependent interaction above pH 7.5. The implications of this finding for the regulation of this Ca2+-activated protein kinase are briefly discussed.

📜 SIMILAR VOLUMES

Radiometric assay of S-adenosylmethionin

Radiometric assay of S-adenosylmethionine:calmodulin(lysine)N-methyltransferase by Calcium-dependent hydrophobic interaction chromatography

✍ Paul M. Rowe; Timothy J. Murtaugh; Wendy L. Bazari; Margaret Clarke; Frank L. Si 📂 Article 📅 1983 🏛 Elsevier Science 🌐 English ⚖ 801 KB

A radiometric assay for Sadenosylmethionine:calmodulin(lysine)N-methyltransferase in tissue extracts has been developed. This assay utilizes the non-N-methylated calmodulin from Dictyostelium discoideum as a substrate and calciumdependent hydrophobic interaction chromatography to isolate the reactio

Comparative modeling studies of the calm

Comparative modeling studies of the calmodulin-like domain of calcium-dependent protein kinase from soybean

✍ Aalim M. Weljie; Teresa E. Clarke; André H. Juffer; Alice C. Harmon; Hans J. Vog 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 479 KB 👁 2 views

Calmodulin-like domain protein kinases (CDPKs) represent a new class of calciumdependent protein-phosphorylating enzymes that are not activated by calmodulin or phospholipid compounds. They have been found exclusively in plant and protozoal tissues. CDPKs are typified by four distinct domains: an N-

Galantamine enhancement of long-term pot

Galantamine enhancement of long-term potentiation is mediated by calcium/calmodulin-dependent protein kinase II and protein kinase C activation

✍ Shigeki Moriguchi; Norifumi Shioda; Feng Han; Jay Z. Yeh; Toshio Narahashi; Kohj 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 652 KB

## Abstract Galantamine, a novel Alzheimer's drug, is known to inhibit acetylcholinesterase activity and potentiate nicotinic acetylcholine receptor (nAChR) in the brain. We previously reported that galantamine potentiates the NMDA‐induced currents in primary cultured rat cortical neurons. We now s

Renaturation of Calcium/Calmodulin-Depen

Renaturation of Calcium/Calmodulin-Dependent Protein Kinase Activity after Electrophoretic Transfer from Sodium Dodecyl Sulfate-Polyacrylamide Gels to Membranes

✍ D.A. Shackelford; J.A. Zivin 📂 Article 📅 1993 🏛 Elsevier Science 🌐 English ⚖ 824 KB

A method is described for analyzing calcium/calmodulin-dependent protein kinase activity in crude or purified samples separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electrophoretically transferred to PVDF membrane. The blotted protein is denatured in situ with guanidine \

Use of Hydrophobic Interaction Chromatog

Use of Hydrophobic Interaction Chromatography to Separate Recombinant Antibody Fragments from Associated Bacterial Chaperone Protein GroEL

✍ Kevin C. O'Connor; Shibnath Ghatak; B.David Stollar 📂 Article 📅 2000 🏛 Elsevier Science 🌐 English ⚖ 59 KB

Activation of calcium/calmodulin-depende

Activation of calcium/calmodulin-dependent protein kinase IV and peroxisome proliferator-activated receptor γ coactivator-1α signaling pathway protects against neuronal injury and promotes mitochondrial biogenesis in the hippocampal CA1 subfield after transient global ischemia

✍ Shang-Der Chen; Tsu-Kung Lin; Jui-Wei Lin; Ding-I Yang; Su-Ying Lee; Fu-Zen Shaw 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 481 KB 👁 1 views

## Abstract Delayed neuronal cell death occurs in the vulnerable CA1 subfield of the hippocampus after transient global ischemia (TGI). We demonstrated previously, based on an experimental model of TGI, that the significantly increased content of oxidized proteins in hippocampal CA1 neuron was obse