Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.22.25 (chymopapain)
 430 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The proteinases from Carica papaya include papain, isoenzymes of chymopapain and two proteinases A and B distinguished by their unusually high pI. The identity of one of the most basic proteinases has been questioned. The present report describes the preparation and characterisation of two monoclonal antibodies that react specifically with papaya proteinases A and B respectively and a third that identifies a common structural feature found in papain and proteinase A.
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PMID:Monoclonal antibodies to the two most basic papaya proteinases. 354 14

Chymotrypsin/elastase inhibitor-1 is a member of the Ascaris family of serine protease inhibitors. It is characterized by five disulfide bridges in a polypeptide chain of 63 amino acids. The disulfide bridge pairing was resolved by cleavage at methionyl residues with cyanogen bromide followed by a combination of proteolytic digestions with glycyl endopeptidase, Staphylococcal serine proteinase, and submandibular proteinase A. The peptides were separated on a reverse-phase HPLC column. Amino acid analyses and N-terminal microsequencing of the cystine containing peptides revealed the disulfide bridge pairing between residues 5-54, 15-29, 18-38, 22-33, and 40-60. The disulfide bridge pairing of other members of this unique family was also assigned. The major isoform, trypsin inhibitor-1, and chymotrypsin/elastase inhibitor-4 share the same disulfide bridge pattern. These results strongly suggest that all members of the Ascaris family of serine protease inhibitors have the same disulfide bridge pattern which represents a unique motif.
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PMID:The serine protease inhibitor family from Ascaris suum: chemical determination of the five disulfide bridges. 851 22