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Abstract

  1. Top of page
  2. Abstract
  3. REFERENCES

A casein kinase was highly purified from rabbit skeletal muscle whose substrate specificity and enzymatic properties were virtually identical to those of casein kinase-I from rabbit reticulocytes. Prolonged incubation of glycogen synthase with high concentrations of skeletal muscle casein kinase-I and Mg-ATP resulted in the incorporation of >6 mol phosphate/mol subunit and decreased the activity ratio (∓ glucose-6P) from 0.8 to <0.02. The sites phosphorylated by casein kinase-I were all located in the N and C-terminal cyanogen bromide peptides, termed CB-1 and CB-2. At an incorporatio of 6 mol phosphate/mol subunit, ∼2 mol/mol was present in CB-1 and ∼4 mol/mol in CB-2. Within CB-1, casein kinase-I phosphorylated the serines that were 3, 7 and 10 residues from the N-terminus of glycogen synthase, with minor phosphorylation at threonine-5. Within CB-2, ∼9% of the phosphate incorporated was located between residues 28 and 53, and at least five of the seven serine residues in this region were phosphorylated. The remaining 10% of phosphate incorporated into CB-2 was located between residues 98 and 123, mainly at a serine residue(s).

Two of the major sites labelled by casein kinase-I (serine-3 and serine-10 of CB-1) are not phosphorylated by any other protein kinase. This will enable the role of casein kinase-I as a glycogen synthase kinase in vivo to be evaluated.

Abbreviations
SDS

sodium dodecyl sulphate

HPLC

high-performance liquid chromatography

Enzymes
 

Glycogen phosphorylase (EC 2.4.1.1)

 

glycogen synthase (EC 2.4.1.11)

 

phosphorylase kinase (EC 2.7.1.38)

 

glycogen synthase kinase and casein kinases-I and II (EC 2.7.1.37)

 

acetyl-CoA carboxylase (EC 6.4.1.2)

 

ATP-citrate lyase (EC 4.1.3.8)

 

trypsin (EC 3.4.21.4)

 

chymotrypsin (EC 3.4.21.1)

 

lysine-specific proteinase (EC 3.4.99.3)

REFERENCES

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  2. Abstract
  3. REFERENCES
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