Literature DB >> 3639830

Elastinolytic activity of horse leukocyte proteinases. Comparison with elastases from human leukocytes and porcine pancreas.

J Potempa, E Korzus, A Dubin, J Silberring.   

Abstract

Three proteinases from the azurophilic granules of horse leucocytes are typical elastases degrading elastin at neutral pH. Both proteinases: 1 and 2A exhibit similar elastinolytic activity, comparable with human leucocyte elastase (HLE). In relation to human enzyme, elastase 2B shows several-fold higher activity, which is comparable to the porcine pancreatic elastase activity (PPE). Similarly to HLE elastinolytic activity of the horse proteinases increases at higher ionic strength: twofold in case of 1 or 2A and fivefold for 2B. Significant activity observed during degradation of homologous lung elastin, implies the possible role of these enzymes during pathological injury of connective tissue in the lower respiratory tract and suggests similar pathogenesis of horse and human pulmonary emphysema.

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Year:  1986        PMID: 3639830

Source DB:  PubMed          Journal:  Folia Histochem Cytobiol        ISSN: 0239-8508            Impact factor:   1.698


  3 in total

1.  Comparative properties of three functionally different but structurally related serpin variants from horse plasma.

Authors:  J Potempa; J K Wunderlich; J Travis
Journal:  Biochem J       Date:  1991-03-01       Impact factor: 3.857

2.  Molecular cloning and expression of an intracellular serpin: an elastase inhibitor from horse leucocytes.

Authors:  T Kordula; A Dubin; H Schooltink; A Koj; P C Heinrich; S Rose-John
Journal:  Biochem J       Date:  1993-07-01       Impact factor: 3.857

3.  Structural and functional characterization of elastases from horse neutrophils.

Authors:  A Dubin; J Potempa; J Travis
Journal:  Biochem J       Date:  1994-06-01       Impact factor: 3.857

  3 in total

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