Amino acid sequence and disulfide bridges of an antifungal protein isolated from Aspergillus giganteus
- 1 October 1990
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 193 (1) , 31-38
- https://doi.org/10.1111/j.1432-1033.1990.tb19300.x
Abstract
A very basic secreted protein which displays antifungal activity was isolated from the medium of the mold A. giganteus. The protein consists of 51 amino acid residues whose sequence was determined as Ala -Thr-Tyr-Asn-Gly-Lys-Cys-Tyr-Lys-Lys-Asp-Asn-Ile-Cys-Lys-Tyr-Lys-Ala-Gln-Ser-Gly-Lys-Thr-Ala-Ile-Cys-Lys-Cys-Tyr-Val-Lys-Lys-Cys-Pro-Arg-Asp-Gly-Ala-Lys-Cys-Glu-Phe-Asp-Ser-Tyr-Lys-Gly-Lys-Cys-Tyr-Cys. Disulfide bonds were formed between Cys7-Cys33, Cys14-Cys40, Cys26-Cys28 and Cys49-Cys51. These results suggest that the antifungal protein forms a loop structure and is similar to phospholipase A2.This publication has 13 references indexed in Scilit:
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