Modified maxadilan protein, its preparation and use, and DNA enc

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

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435 691, 435 697, 435214, 435217, 514 12, 530300, 530324, 536 221, 536 231, 536 232, 536 234, 536 235, 536 241, A61K 3800, C12P 2106, C12N 948, C07H 1900

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active

054808642

ABSTRACT:
A modified maxadilan protein exhibits higher biological activity than native maxadilan from the sand fly Lutzomyia longipalpis. A modified maxadilan fusion protein contains a thrombin cleavage site. This enables the production of the modified maxadilan as a fusion protein and recovery of the modified maxadilan after digestion with thrombin. The modified maxadilan is a potent vasodilator.

REFERENCES:
International Search Report PCT/US94/08809 Lerner et al., Ethan A., "Maxadilan Cloning and Functional Expression of the Gene Encoding This Potent Vasodilator Peptide," J. Bio. Chem., vol. 267, No. 2, pp. 1062-1066 (1992).
Mandel, M., et al., Calcium-dependent Bacteriophage DNA Infection, J. Mol. Biol., 53:159-162 (1970).
Lerner, E., et al., Maxadilan--Cloning and Functional Expression of the Gene Encoding This Potent Vasodilator Peptide, Journal of Biological Chemistry, vol. 267, No. 2, Issue of Jan. 15, 1992, pp. 1062-1066.
Smith D., et al., Single-step Purification of Polypeptides Expressed in Escherichia coli as Fusions with Glutathione S-transferase, Gene, vol. 67, No. 1, Issue of Jul. 15, 1988, pp. 31-40.
Ribeiro et al., A Novel Vasodilatory Peptide from the Salivary Glands of the Sand Fly Lutzomyia longipalpis, Science, vol. 243, pp. 212-214 (1989).
Chang, Thrombin specificity--Requirement for Apolar Amino Acids Adjacent to the Thrombin Cleavage Site of Polypeptide Substrate, Eur. J. Biochem., vol. 151, pp. 217-224 (1985).

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