1988
DOI: 10.1016/0014-5793(88)80820-2
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The disulfide bridges of the immunoreactive forms of human pancreatic stone protein isolated from pancreatic juice

Abstract: Following the complete sequence elucidation of human pancreatic stone protein (immunoreactive form PSP S1 isolated from pancreatic juice) [(1987) Eur. J. Biochem. 168, 201-207], the location of the three S-S bridges of the protein was investigated. The cystine-containing peptides, detected after the separation of the peptic or chymotryptic digests on SP-Sephadex or Sephadex G-50, were submitted to Edman degradation and/or to oxidation. The cysteic peptides after separation on SP-Sephadex or Sephadex G-50 were … Show more

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Cited by 17 publications
(1 citation statement)
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“…The 5 half-cystine residues in MBP here shown to possess free sulfhydryl groups are all unique compared to other members of the animal lectin family, exemplified by the structure of human pancreatic stone protein and tetranectin [25,26]. In contrast to MBP, no other member is believed to contain free thiol groups.…”
Section: Discussionmentioning
confidence: 93%
“…The 5 half-cystine residues in MBP here shown to possess free sulfhydryl groups are all unique compared to other members of the animal lectin family, exemplified by the structure of human pancreatic stone protein and tetranectin [25,26]. In contrast to MBP, no other member is believed to contain free thiol groups.…”
Section: Discussionmentioning
confidence: 93%