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 complete amino acid sequence of bovine spleen cathepsin S has been determined. The single-chain protein contains 217 residues and has a Mr of 23,682. The primary structure was determined by sequencing of native protein and the peptides obtained by proteolytic cleavage with beta-trypsin, papaya proteinase IV and by chemical cleavage with cyanogen bromide. Comparison of the amino terminal sequences of the heavy and the light chain of bovine cathepsin L with that of bovine cathepsin S clearly indicates that the enzymes are structurally different.
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PMID:The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L. 204 74

The amino acid sequence of a cathepsin D inhibitor isolated from potato is described. It was determined by analysis of peptides generated by use of the glycine-specific proteinase PPIV. The order of the peptides was established by examination of tryptic peptides derived from the two cyanogen bromide peptides. The inhibitor comprises 187 amino acid residues, and has a calculated Mr of 20,450.
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PMID:The amino acid sequence of a novel inhibitor of cathepsin D from potato. 236 79

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

Cathepsin L and stefin B were isolated from sheep liver, the cathepsin L being isolated by a low pH homogenisation method, which increases the proportion of the two-chain form of the enzyme, thus facilitating sequencing. The amino acid sequences of the isolated cathepsin L and stefin B were determined. The two-chain form of cathepsin L contains 217 amino acid residues and has an M(r) of 23,627. The sequence was obtained by sequencing the native active enzyme, the light and heavy chains and the peptides generated by cyanogen bromide cleavage. These peptides were aligned with peptides obtained by hydrolysis with endoproteinase Lys-C, glycyl endopeptidase and endoproteinase Glu-C. Sheep liver cathepsin L exhibits a high degree of sequence identity to human cathepsin L. Sheep stefin B consists of 98 amino acid residues and its calculated M(r) is 11,150. The inhibitor has its NH2-terminal amino acid residue blocked. Its amino acid sequence was determined by sequencing the peptides obtained by cleavage with cyanogen bromide and peptides obtained by hydrolysis with endoproteinase Glu-C and endoproteinase Lys-C. Sheep stefin B shows a high degree of sequence identity with bovine and human stefin B. The kinetics of the interaction between sheep cathepsin L and stefin B were determined, with the interaction of stefin B with papain used as a benchmark to compare with other published results. Despite the considerable homology between bovine and sheep stefin B, the kinetics of their interaction with papain and cathepsin L differed markedly, possibly due to the differences in the so-called "trunk" region of the cystatin molecule.
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PMID:The amino acid sequences, structure comparisons and inhibition kinetics of sheep cathepsin L and sheep stefin B. 875 91