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2 Acta Biochimica Polonica

2 1996

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Biosythesis and distibution of leucocyte elastase inhibitor. Production of recombinant in inhibitor

100%

Kasza A. , Korpula-Mastalerz R. , Rose-John S. , Dubin A.

Acta Biochimica Polonica

1996

tom 43

nr 3

The horse leucocyte elastase inhibitor (HLEI), present in neutrophils, monecytes and bone marrow cells, is apparently a cytoplasmic protein which is not released from cells even in response to stimulation with lipopolysaccharide, phorbol ester, tumour necrosis factor alpha, interleukin-1 or elastin degradation products. Although no expression of the inhibitor was detected in neutrophils, both monocytes and bone marrow cells were efficient in its synthesis. Using a new expression vector pREST5d, recombinant inhibitor was produced in a large quantity in a soluble form, with a yield of 88 mg per 10 litres of E. colt culture. A two-step purification procedure, consisting of ion-exchange chromatography and gel filtration, yielded 36 mg of the recombinant inhibitor of a purity higher than 95%, as judged by SDS/PAGE. The recombinant protein had physicochemical and kinetic properties indistinguishable from those of the natural one, including irreversible elastase inhibition with an association rate constant kass > 10 7 M -1 s -1. Both proteins were eliminated from rat circulation at the same ratio, and within the first 20 min 70% of the protein was removed. Such a short half-life in the circulation suggests that local delivery of HLEI directly to lungs in the form of aerosol could be a more efficient therapeutic approach than its intravenous injection.

The intracellular serpin family

86%

Korpula-Mastalerz R. , Dubin A.

Acta Biochimica Polonica

1996

tom 43

nr 3

The serpins are widely distributed, structurally related family of proteins with diverse functions. Most of the known serpins are proteinase inhibitors, the majority being found as secreted species, however, there are a few that occur intracellularly and their physiological role remains unknown. Most of the intracellularly occuring serpins have been classified into the ovalbumin subfamily. The possible phytogenetic tree of 14 intracellular serpins is presented.