Literature DB >> 400950

Schistosoma mansoni: inhibition of cercarial "penetration" proteases by components of mammalian blood.

H L Asch1, M H Dresden.   

Abstract

1. Normal human sera and plasma were fractionated in order to identify inhibitors of the "penetration" proteases of Schistosoma mansoni cercariae. 2. The main inhibitor, accounting for 90% of the total activity of serum, appears to be alpha 1-antitrypsin (alpha 1-AT) as identified by separation on DEAE-cellulose and Sephadex, by immunoelectrophoresis and by anticercarial protease activity of purified alpha 1-AT preparations. 3. The inhibition profiles of purified preparations of the 6 known serum antiproteases suggest that the parasite protease is similar to vertebrate chymotrypsin. 4. On a molar basis, the order of inhibitory activity against the cercarial protease is: alpha 1-AT = alpha 2-macroglobulin; C'-1-inactivator; alpha 1-antichymotrypsin. No inhibition was obtained with inter-alpha-inhibitor or antithrombin III.

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Year:  1977        PMID: 400950     DOI: 10.1016/0305-0491(77)90132-8

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  2 in total

Review 1.  Proteases in the schistosome life cycle: a paradigm for tumour metastasis.

Authors:  M J Doenhoff; R H Curtis; J Ngaiza; J Modha
Journal:  Cancer Metastasis Rev       Date:  1990-12       Impact factor: 9.264

2.  Purification and properties of a proteolytic enzyme from the cercariae of the human trematode parasite Schistosoma mansoni.

Authors:  W J Landsperger; M A Stirewalt; M H Dresden
Journal:  Biochem J       Date:  1982-01-01       Impact factor: 3.857

  2 in total

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