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Synthetic Myelin Basic Protein Peptide Analogs Are Specific Inhibitors of phospholipid/calcium-dependent Protein Kinase (Protein Kinase C)

H D Su, B E Kemp, R S Turner, J F Kuo

Biochem Biophys Res Commun. 1986 Jan 14;134(1):78-84.

PMID: 2418828

Abstract:

Synthetic peptide analogs of the bovine myelin basic protein (MBP) corresponding to residues 104-118 were found to specifically inhibit phospholipid/ Ca2+-dependent protein kinase (protein kinase C). The peptides [Ala107]MBP (104-118) and [Ala113]MBP (104-118) inhibited protein phosphorylation of intact MBP, histone H1 and peptide phosphorylation with MBP(104-123), MBP(104-118) or [Ala105]MBP (104-118) as substrates. The inhibitor peptides [Ala107]MBP(104-118) and [Ala113]MBP (104-118), containing alanine in place of the arginine recognition sites, apparently inhibited the enzyme noncompetitively with respect to substrates, with IC50 values ranging from 46-145 and 28-62 microM, respectively. These peptide analogs did not inhibit cyclic AMP-dependent protein kinase or myosin light chain kinase but inhibited phospholipid/Ca2+-dependent phosphorylation of endogenous proteins in the total, solubilized fraction of rat brain.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR42416422 [Ala107]-Myelin Basic Protein Fragment 104-118 [Ala107]-Myelin Basic Protein Fragment 104-118 Price
IAR4244032 [Ala113]-Myelin Basic Protein Fragment 104-118 [Ala113]-Myelin Basic Protein Fragment 104-118 Price
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