Evidence for a cysteine-histidine thioether bridge in functional units of molluscan haemocyanins and location of the disulfide bridges in functional units d and g of the betaC-haemocyanin of Helix pomatia.

Abstract

In functional units d and g from the betaC-haemocyanin of the gastropod Helix pomatia, aminoacid analysis in the presence of dimethyl sulfoxide showed the occurrence of seven cysteine residues. Titration with 5,5'-dithiobis(2-nitrobenzoic acid), however, did not reveal any free thiol group. Pepsinolysis at pH 2.0 followed by amino acid analysis and partial… (More)

Topics

Cite this paper

@article{Gielens1997EvidenceFA, title={Evidence for a cysteine-histidine thioether bridge in functional units of molluscan haemocyanins and location of the disulfide bridges in functional units d and g of the betaC-haemocyanin of Helix pomatia.}, author={Constant Gielens and Natalie de Geest and Xue Qian Xin and Bart Devreese and Jozef J. Van Beeumen and Gis{\`e}le Pr{\'e}aux}, journal={European journal of biochemistry}, year={1997}, volume={248 3}, pages={879-88} }