Apr 14, 1976

Isolation, characterization and partial sequence of cyanogen bromide fragments and thiol peptides from pig kidney D-amino-acid oxidase

Biochimica Et Biophysica Acta
S RonchiJ Bridgen

Abstract

A partial characterization of the primary structure of D-amino-acid oxidase (D-Amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3.) from hog kidney has been achieved by a CNBr cleavage of the 14C-carboxymethylated protein. Four fragments have been isolated and purified and their alignment made possible by overlapping with methionine-containing peptides derived from tryptic digestion of the 14C-carboxymethylated protein. A partial sequencing of the CNBr fragments has been carried out by the automated Edman procedure and by manual sequence analysis. Chymotryptic peptides containing the 5 alkylated thiols of the monomer enzyme (Curti, B., Ronchi, S., branzoli, U., Ferri, G. and Williams, Jr., C. H. (1973) Biochim. Biophys. Acta 327, 266-273) have been isolated and their sequence determined. The present results do not show any significant homologies with the known sequences of other flavoproteins.

  • References3
  • Citations7

References

  • References3
  • Citations7

Mentioned in this Paper

D-Amino Acid Dehydrogenase
DAO gene
Cytokinesis of the Fertilized Ovum
Sulfhydryl Compounds
Kidney
Flavoproteins
Plasma Protein Binding Capacity
Bromides Measurement
Sequence Analysis
Sequencing

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