Glycosaparaginase from human leukocytes. Inactivation and covalent modification with diazo-oxonorvaline.

This publication has 25 references indexed in Scilit:

• The turnover of lysosomal glycosylasparaginase in rat liver
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
• Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 l-asparaginase gene
  Gene, 1985
• Quantitative analysis, by gas-liquid chromatography and mass fragmentography, of monosaccharides after methanolysis and deamination
  Carbohydrate Research, 1981
• Two species of lysosomal organelles in cultured human fibroblasts
  Cell, 1979
• Amino acid sequence of the diazooxonorleucine binding site of Acinetobacter and Pseudomonas 7 A glutaminase-asparaginase enzymes
  Biochemistry, 1978
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• The purification and properties of a β-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct
  Archives of Biochemistry and Biophysics, 1969
• Mass spectrometry of permethylated peptide derivatives; extension of the technique to peptides containing arginine or methionine
  Biochemical and Biophysical Research Communications, 1968
• 5-Diazo-4-Oxo-L-Norvaline: Reactive Asparagine Analog with Biological Specificity
  Science, 1968
• 390. The standardisation of some buffer solutions at elevated temperatures
  Journal of the Chemical Society, 1937