Changes in the structure and chemistry of beta-lactoglobulin (beta-LG) play an important role in the processing and functionality of milk products. In model beta-LG systems, there is evidence that the aggregates of heated beta-LG are held together by a mixture of intermolecular non-covalent association and heat-induced non-native disulfide bonds. Although a number of non-native disulfide bonds ...

μ-Conotoxin GIIIA, a peptide toxin isolated from Conus geographus, preferentially blocks the skeletal muscle sodium channel NaV1.4. GIIIA folds compactly to a pyramidal structure stabilized by three disulfide bonds. To assess the contributions of individual disulfide bonds of GIIIA to the blockade of NaV1.4, seven disulfide-deficient analogues were prepared and characterized, each with one, two...

The functional structure of gamma globulins and antibodies has recently come under intensive investigation through the use of reduction and alkylation of disulfide bonds (1). This method has revealed the great similarity in fundamental polypeptide chain structure among many species as well as between the different classes of immunoglobulins (2). By contrast, reduction of disulfide bonds affects...

We have synthesized a new reagent-N,N'-dimethyl-N,.,V.bis(mercaptoacetyl)hydrazine(DMH)-for the reduction of disulfide bonds in proieins. DMH reduce.s disulfide bonds ? times faster than does dithiothreitol (DTT) in water at pH ?. DMH reduces mixed disulfides of cvsteine proteases (papain and ficin) especially rapdily i30 ti-.r faster than DTT). DMH (eo = -0.300 V) reduces noncl'clic disulfides...

BACKGROUND Disulfide bonds are the most common structural, post-translational modification found in proteins. Antibodies contain up to 25 disulfide bonds depending on type, with scFv fragments containing two disulfides and Fab fragments containing five or six disulfide bonds. The production of antibody fragments that contain native disulfide bonds can be challenging, especially on a large scale...

Plasma plasminogen is the precursor of the tumor angiogenesis inhibitor, angiostatin. Generation of angiostatin in blood involves activation of plasminogen to the serine protease plasmin and facilitated cleavage of two disulfide bonds and up to three peptide bonds in the kringle 5 domain of the protein. The mechanism of reduction of the two allosteric disulfides has been explored in this study....