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1: Biol Chem Hoppe Seyler. 1990 May;371 Suppl:295-304.Links
Erratum in:
Biol Chem Hoppe Seyler 1990 Aug;371(8):733.

Partial amino acid sequence of human PMN leukocyte procollagenase.

University of Bielefeld, Faculty of Chemistry, Department of Biochemistry, FRG.

Human PMN leukocyte procollagenase was purified to apparent homogeneity using ion exchange chromatography on Q-Sepharose Fast Flow, affinity chromatography on Zinc Chelate Sepharose and on Orange Sepharose and was finally purified by gelpermeation chromatography on Sephacryl S-300. It was shown by SDS-PAGE under reducing and non-reducing conditions that PMNL procollagenase consists of a single polypeptide chain with an apparent Mr 85000. Amino acid sequence information was obtained from the proenzyme and fragments by Edman degradation and showed that PMNL procollagenase is homologous to the fibroblast enzyme. Thus PMNL procollagenase is the product of an independent gene.

PMID: 2169256 [PubMed - indexed for MEDLINE]