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Literature summary for 2.4.1.1 extracted from

  • Makino, Y.; Omichi, K.
    Sensitive assay of glycogen phosphorylase activity by analysing the chain-lengthening action on a fluorogenic [corrected] maltooligosaccharide derivative (2009), J. Biochem., 146, 71-76.
    View publication on PubMed
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Application

Application Comment Organism
analysis a highly sensitive and convenient assay for glycogen phosphorylase activity by analysing its chainlengthening action on a fluorogenic maltooligosaccharide derivative in a glucose-1-phosphate-rich medium. A maltotetraosyl residue comprising the non-reducing-end of a pyridylaminated maltooligosaccharide is indispensable for the chain-lengthening action of phosphorylase, and pyridylaminated maltohexaose is the most suitable substrate. Pyridylaminated maltoheptaose produced by the chain elongation reaction can be isolated and quantified at 10 fmol. Method has about 1000 times greater sensitivity than the spectrophotometric phosphate assay Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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Source Tissue

Source Tissue Comment Organism Textmining
muscle
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 Oryctolagus cuniculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information a maltotetraosyl residue comprising the non-reducing-end of a pyridylaminated maltooligosaccharide is indispensable for the chain-lengthening action of phosphorylase Oryctolagus cuniculus ?
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