A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal "protective protein".

This publication has 44 references indexed in Scilit:

• Substance P primes human neutrophil activation: A mechanism for neurological regulation of inflammation
  Biochemical and Biophysical Research Communications, 1989
• Expression of cDNA encoding the human “protective protein≓ associated with lysosomal β-galactosidase and neuraminidase: Homology to yeast proteases
  Cell, 1988
• Release of immunoreactive-neuropeptide Y by rat platelets
  Biochemical and Biophysical Research Communications, 1988
• Conversion of Angiotensin I to Angiotensin II by cathepsin A isoenzymes of porcine kidney
  Biochemical and Biophysical Research Communications, 1988
• Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: comparison with other carboxypeptidases
  Biochemical and Biophysical Research Communications, 1988
• Basic carboxypeptidases: regulators of peptide hormone activity
  Trends in Pharmacological Sciences, 1988
• The involvement of platelets in non-thrombotic processes
  Trends in Pharmacological Sciences, 1988
• Action of serine carboxypeptidases on endopeptidase substrates, peptide‐4‐methyl‐coumaryl‐7‐amides
  European Journal of Biochemistry, 1985
• Enzymatic deamidation of the C-terminal tetrapeptide amide of gastrin by mammalian tissues
  Biochemical Medicine, 1973
• NATURE OF LYSOSOMAL ANGIOTENSINASE ACTIVITY
  Japanese Circulation Journal, 1971