Book ReviewCope's Early Diagnosis of the Acute Abdomen

Johnson, Mayo

doi:10.1056/nejm198711263172217

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Synthetic Hexapeptide Assay1

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1994

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“…This is a modified version of the assay described in [15] using the substrate Ac-Pro-Gln-Gly-Leu-Leu-Gly-OEt.…”

Section: Synthetic Hexapeptide Assaymentioning

confidence: 99%

Specific amino acid substitutions in human collagenase cause decreased autoproteolysis and reveal a requirement for a second zinc atom for catalytic activity

Williams

Murray

1994

FEBS Letters

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We have previously reported the crystal structure of truncated human collagenase (domain II) complexed with a low molecular weight inhibitor. Attempts to crystallise full-length active collagenase (i.e. domain II + III) have been hindered by autoproteolysis at the domain II/III junction at high protein concentrations. To overcome this problem, we have generated an inactive enzyme via a H149-1 L,D151 +N double substitution which displaces the non-catalytic zinc atom, and shown that the altered collagenase is unable to cleave a synthetic substrate. We have also generated an 1251 +S substitution at the domain II/III junction and demonstrate an increased resistance to proteolysis compared to wild-type collagenase.

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“…This is a modified version of the assay described in [15] using the substrate Ac-Pro-Gln-Gly-Leu-Leu-Gly-OEt.…”

Section: Synthetic Hexapeptide Assaymentioning

confidence: 99%