Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.27 (thermolysin)
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Decay accelerating factor (DAF) has 4 SCR (short consensus repeat) units. Each SCR unit consists of approx. 60 amino acids characterized by having four conserved cysteine residues and several other highly conserved residues which include proline, tryptophan, tyrosine/phenylalanine and glycine. To determine the disulfide-bonding pattern, we used the urine form of DAF. After thermolysin and trypsin digestion, we isolated seven disulfide-linked peptides by HPLC purification. Because all of the cysteine residues are disulfide-bonded, DAF should contain eight disulfide bonds. After subtilisin and trypsin digestion, we isolated the eighth disulfide-bonded peptides by HPLC purification. From sequence analyses of these peptides, we could identify all disulfide bonds in the 4 SCR units of DAF as being between the first and the third and between the second and the fourth half-cystines within each SCR unit.
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PMID:Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen). 137 29

C1s, one of the three subcomponents of C1, the first component of the complement system, is a complex serine protease. To determine the disulfide-bonding pattern, fragments of C1s were generated by cleavage with pepsin, thermolysin, or subtilisin. Disulfide bonds have been identified by several methods, for example, direct observation of the phenylthiohydantoin derivative of cystine during Edman degradation of isolated peptides and placement in the known cDNA sequence. All of the 26 half-cystines are linked in disulfide bonds occurring at positions 50-68, 120-132, 128-141, 143-156, 160-187, 219-236, 279-326, 306-339, 344-388, 371-406, 410-534, 580-603, and 613-644. All of the disulfide bonds of the earlier described substructures of C1s, the EGF-homologous part, the two SCR units, and the two domains typical for C1s and C1r are localized within these domains.
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PMID:Identification of the disulfide bonds of human complement C1s. 200 22