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Isolation of S-100 Binding Proteins From Brain by Affinity Chromatography

Isolation of S-100 Binding Proteins From Brain by Affinity Chromatography

R Gopalakrishna, S H Barsky, W B Anderson

Biochem Biophys Res Commun. 1985 May 16;128(3):1118-24.

PMID: 2988527

Abstract:

S-100-binding proteins, and calmodulin-binding proteins were isolated from S-100- and calmodulin-depleted bovine brain extract by Ca2+-dependent affinity chromatography using S-100- and calmodulin-coupled Sepharose columns respectively. The majority of the protein (80 to 90%) including calcineurin that bound to S-100 also bound to calmodulin and vice versa, suggesting both proteins may regulate common targets. However these two regulatory proteins also bind few other proteins specific for each. These include cyclic nucleotide phosphodiesterase, 55k, and 220k proteins for calmodulin and 24k, 42k, and 90k proteins for S-100. Certain proteins also specifically bound to S-100 both in Ca2+-dependent and independent ways. In glial cells S-100 protein may replace calmodulin in regulating Ca2+-influenced functions.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4248909	S-100B Protein from bovine brain			Price

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