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Active site peptides from glycogen phosphorylase
- Source :
- Biochemical and biophysical research communications. 39(5)
- Publication Year :
- 1970
-
Abstract
- The isolation and sequence of active site peptides from glycogen phosphorylase b is described. These cysteine peptides become exposed to preferential labeling upon removal of pyridoxal 5′-phosphate (PLP) from the enzyme and they have the sequence Ala-Cys, Asx-Ala-Cys-Asp and Asx-Glx-Lys-Cys-Gly-Gly. The first two of these peptides appear to be derived from the PLP binding site of phosphorylase.
- Subjects :
- Electrophoresis
Paper
Chromatography, Paper
Biophysics
Biochemistry
Glycogen phosphorylase
chemistry.chemical_compound
Glycogen branching enzyme
Amino Acid Sequence
Pyridoxal phosphate
Amino Acids
Glycogen synthase
Phosphorylase kinase
Molecular Biology
Peptide sequence
Carbon Isotopes
Binding Sites
biology
Glycogen
Active site
Cell Biology
chemistry
Glucosyltransferases
Pyridoxal Phosphate
biology.protein
Chromatography, Gel
Solvents
Cystine
Colorimetry
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 39
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....c347330fe7087c1773ac0419eddba406