These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Activation of latent collagenase purified from human leukocytes.
    Author: Sorsa TA.
    Journal: Scand J Rheumatol; 1987; 16(3):167-75. PubMed ID: 3037686.
    Abstract:
    Latent human leukocyte collagenase was isolated to apparent homogeneity by a simple and rapid method. Isolation was accomplished by gel filtration on Sepharose 6B and ion exchange chromatography on QAE Sephadex A-50 followed by affinity chromatography on Cibacron Blue Sepharose. The purified latent enzyme exhibits an apparent molecular weight of 70 kD as estimated by SDS-polyacrylamide gel electrophoresis. Reduction with dithiothreitol does not change the mobility of the latent human leukocyte collagenase on SDS-polyacrylamide gel electrophoresis, indicating that the enzyme consists of a single polypeptide chain. The enzyme could be activated by trypsin and thiol reagents such as phenylmercuric chloride and N-ethylmaleimide. Upon activation by trypsin a 54 kD polypeptide was formed from the 70 kD latent enzyme. Concomitant with the activation by thiol reagents, no loss of molecular weight was detected. Inactivated trypsin, i.e. phenylmethyl sulfonyl-trypsin or soybean trypsin inhibitor treated trypsin, was not able to activate latent human leukocyte collagenase. The results support the concept that latent human leukocyte collagenase exists as a proenzyme and thiol-dependent activation occurs through conformational perturbation in the proenzyme molecule.
    [Abstract] [Full Text] [Related] [New Search]