Method for identifying and producing a protease capable of cleav

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

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435226, 530350, 530327, 530328, C12N 950, C12N 964

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active

057669171

ABSTRACT:
Molecules which influence the shedding of the cell-bound p55 Tumor Necrosis Factor receptor (p55-TNF-R), are provided, together with methods of producing them.

REFERENCES:
Angelo, et al, "Elastatinal, A-PMSF, and pepstatin inhibit p80 tumor necrosis factor receptor (TNF-R) shedding in activated human lymphocytes", Proceedings of the American Association for Cancer Research; 34:441 (1993).
Ehlers, et al, "Membrane Proteins with Soluble Counterparts: Role of Proteolysis in the Release of Transmembrane Proteins", Biochemistry; 30(42):10065-10074 (1991).
Gary, et al, "Cloning of human tumor necrosis factor (TNF) receptor cDNA and expression of recombinant soluble TNF-binding protein", Proceedings of the National Academy of Sciences of the USA; 80(10):7380-7384 (1990).
Gullberg, et al, "Involvement of an Asn/Val cleavage site in the production of a soluble form of a human tumor necrosis factor (TNF) receptor. Site-directed mutagenesis of a putative cleavage site in the p55 TNF receptor chain"; European Journal of Cell Biology; 58:307-312 (1992).
Heimbach, et al, "Affinity purification of the HIV-1 protease", Chemical Abstracts; 112(7)(51017):51022(1990).
Hwang, et al, "A 20 amino acid synthetic peptide f a region from the 55 kDa human TNF receptor inhibits cytolytic and binding activities of recombinant human tumour necrosis factor in vitro", Proc. R. Soc. Land. B; 245:115-119 (1991).
Porteu, et al, "Human Neutrophil Elastase Releases a Ligand-binding Fragment from the 75-kDa Tumor Necrosis Factor (TNF) Receptor", The Journal of Biological Chemistry; 266(28): 18846-18853 (1991).

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