N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein. The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue

  • De Caro A
  • Adrich Z
  • Fournet B
 et al. 
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Abstract

The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond. Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoprotine and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules. Variations in the glycan chain composition account for the differences in the Mrof PSP S2-5. The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble. © 1989.

Author-supplied keywords

  • (Human)
  • Amino acid sequence
  • Amino terminal 5-oxoproline
  • Carbohydrate content
  • O-Glycosyl-bond cleavage
  • Pancreatic calculi
  • Pancreatic stone protein

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Authors

  • Alain M. De Caro

  • Zygmunt Adrich

  • Bernard Fournet

  • Calliope Capon

  • Jacques J. Bonicel

  • Josiane D. De Caro

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