Home
Resources
Publications
Disulfide Bonds of Phospholipase A2 From Bee Venom Yield Discrete Contributions to Its Conformational Stability

Disulfide Bonds of Phospholipase A2 From Bee Venom Yield Discrete Contributions to Its Conformational Stability

Sylvia Welker, Yvonne Markert, Jens Köditz, Johanna Mansfeld, Renate Ulbrich-Hofmann

Biochimie. 2011 Feb;93(2):195-201.

PMID: 20884319

Abstract:

Disulfide bonds are known to be crucial for protein stability. To probe the contribution of each of the five disulfide bonds (C9-C31, C30-C70, C37-C63, C61-C95, and C105-C113) in bee venom phospholipase A(2) to stability, variants with deleted disulfide bonds were produced by substituting two serine residues for each pair of cysteine residues. The mutations started from the pseudo-wild-type variant (pWT) with the mutation I1A (Markert et al., Biotechnol. Bioeng. 98 (2007) 48-59). All variants were expressed in Escherichia coli, refolded from inclusion bodies and purified as pWT. The activity of the variants ranged from 12 to 82% of pWT. From the transition curves of guanidine hydrochloride-induced unfolding, the contributions of the individual disulfide bonds to conformational stability were estimated. They increased in the sequence C9-C31

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001847-A	Phospholipase A2 from bovine pancreas		9001-84-7	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: