| http://purl.uniprot.org/citations/2159879 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2159879 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2159879 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/2159879 | http://www.w3.org/2000/01/rdf-schema#comment | "Procollagenase of human polymorphonuclear leucocytes was purified to homogeneity using a rapid and reproducible method. The purification procedure included affinity chromatography on zinc chelate Sepharose, ion exchange chromatography on Q-Sepharose fast flow, followed by affinity chromatography on orange Sepharose and finally a gel-permeation step on Sephacryl S-300. It was shown by SDS/PAGE, under reducing conditions, that the latent collagenase of human polymorphonuclear leucocytes consists of a single polypeptide chain with an apparent relative molecular mass of 85,000. Upon deglycosylation by endoglycosidase F digestion, the apparent relative molecular mass of the procollagenase was reduced to 53,000 which is similar to that of the fibroblast enzyme, and indicates a close relationship between both enzymes. Sequence data were determined by direct automated Edman degradation of the purified polymorphonuclear leucocyte procollagenase. The complete sequence of the propeptide region (residue 1-120) was thereby established. The proteolytic activation of the polymorphonuclear leucocyte procollagenase by various enzymes was investigated by determining the N-terminal sequences of the intermediate and final activated forms. Activation by chymotrypsin and cathepsin G led to the active form (Mr 64,000) by cleaving 79 N-terminal residues from the proenzyme. Trypsin activates in a two-step process. Cleavage of 48 N-terminal residues led to a still latent Mr 70,000 species. The final active form (Mr 65,000) was obtained by splitting off 20 additional N-terminal residues."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1990.tb15489.x"xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1990.tb15489.x"xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/author | "Reinke H."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/author | "Reinke H."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/author | "Tschesche H."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/author | "Tschesche H."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/author | "Kraemer S."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/author | "Kraemer S."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/author | "Knaeuper V."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/author | "Knaeuper V."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/pages | "295-300"xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/pages | "295-300"xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/title | "Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/title | "Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms."xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/volume | "189"xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://purl.uniprot.org/core/volume | "189"xsd:string |
| http://purl.uniprot.org/citations/2159879 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2159879 |