Calcium-dependent hydrophobic interaction chromatography of calmodulin, troponin C and their proteolytic fragments

Interaction of proteolytic fragments of calmodulin with caldesmon and calponin.

Interaction of five tryptic fragments of calmodulin with caldesmon and calponin was analysed by native gel electrophoresis. In the presence of Ca2+ intact calmodulin interacts with caldesmon and calponin with apparent Kd values equal to 0.23 and 1.3 microM respectively. The interaction was abolished in the absence of Ca2+. Two large tryptic fragments of calmodulin obtained in the presence of Ca...

Hydrophobic Interaction Chromatography

Hydrophobic Interaction Chromatography

modeling for the design of a Biomimetic chimeric ligand. Application to the puriRcation of bovine heart L-lactate dehydrogenase. Biotechnology and Bioengineering 63: 321}331. Lowe CR (1984) Applications of reactive dyes in biotechnology. In: Wiseman A (ed.) Topics in Enzyme and Fermentation Biotechnology, vol. 9. Chichester: Ellis Horwood. Lowe CR, Burton S, Pearson J, Clonis YD and Stead CV (1...

Hydrophobic Interaction Chromatography.

Most proteins and large polypeptides have hydrophobic regions at their surface. These hydrophobic "patches" are due to the presence of the side chains of hydrophobic or nonpolar amino acids such as phenylalanine, tryptophan, alanine, and methionine. These surface hydrophobic regions are interspersed between more hydrophilic or polar regions and the number, size, and distribution of them is a sp...

Calcium-dependent affinity chromatography of S-100 and calmodulin on calmodulin antagonist-coupled Sepharose.

Two different calcium-binding proteins, S-100 and calmodulin, have been isolated from bovine brain by calcium-dependent affinity chromatography on calmodulin antagonist coupled to Sepharose. Calmodulin antagonist N-(6-aminohexyl)-5-chloro-l-napthdenesulfonamide (W-7) has been coupled to epoxy-activated Sepharose 6B or cyanogen bromide-acitivated Sepharose 4B. S-100-like protein bound to W-7 cou...