It was found that, for a dissolving pulp, an enzymatic pre-treatment with an endoglucanase prior to viscose preparation did not change the correlation between the gamma number of the viscose dope and the carbon disulphide charge. Thus, the pulp stoichiometry, or reactivity, was not changed by an endoglucanase pre-treatment. It has nevertheless previously been found that the pulp reactivity, mea...

The formation of disulphide bridges between cysteines plays an important role in protein folding, structure, function, and evolution. Here, we develop new methods for predicting disulphide bridges in proteins. We first build a large curated data set of proteins containing disulphide bridges to extract relevant statistics. We then use kernel methods to predict whether a given protein chain conta...

OBJECTIVE Childhood obesity is an important cause of cardiovascular risk with chronic inflammation. Oxidative stress may contribute to the pathogenesis of obesity-related cardiovascular pathologies. We aimed to evaluate thiol/disulphide homeostasis as a novel and sensitive marker of oxidative stress and to evaluate its relationship with some inflammatory and cardiovascular markers in obese chil...

Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. This review will discuss how these enzymes are maintained in either an oxidiz...

A heterobifunctional reagent, N-succinimidyl 3-(2-pyridyldithio)propionate, was synthesized. Its N-hydroxysuccinimide ester group reacts with amino groups and the 2-pyridyl disulphide structure reacts with aliphatic thiols. A new thiolation procedure for proteins is based on this reagent. The procedure involves two steps. First, 2-pyridyl disulphide structures are introduced into the protein by...

Previously only one of the six disulphide bonds within the βsubunit of bovine thyrotropin (bTSHβ) has been unequivocally assigned. In the present investigation, the fluorescent alkylating reagent 5-N-[(iodoacetamidoethyl)amino]naphthalene-1-sulphonic acid has been employed as part of a double-alkylation strategy to allow the relative reactivities and the location of the six disulphide bonds of ...

Activated carbons are universal adsorbents that can be obtained from a wide variety of raw materials, and have been found to be very effective for mercury removal from water. This contribution presents a comparative adsorption in column study of activated carbons obtained by physical activation of carbonized eucalyptus wood with water vapour, as adsorbents of mercury in liquid phase. Two sampl...

Background Disulphide bonding is critical to maintaining immunoglobulin (IgG) tertiary and quaternary structure for therapeutic monoclonal antibodies (MAb). Both interand intra-chain disulphide bonds are formed intracellularly in the expression host prior to secretion and purification during MAb production processes. Disulphide bond shuffling has previously been reported for IgG2[1,2] and disul...

Trypanothione: glutathione disulphide thioltransferase of Try-panosoma cruzi (p52) is a key enzyme in the regulation of the intracellular thiol-disulphide redox balance by reducing glutathione disulphide. Here we show that p52, like other disulphide oxidoreductases possessing the CXXC active site motif, catalyses the reduction of low-molecular-mass disulphides (hydroxyethyl-disulphide) as well ...

Cytoplasmic thioltransferase purified from rat liver [Axelsson, Eriksson & Mannervik (1978) Biochemistry 17, 2978--2984] catalyses the formation and decomposition of mixed disulphides of proteins and glutathione. The enzyme was found to catalyse the reversible thiol-disulphide interchange between glutathione disulphide and a crude thiol-containing protein fraction from rat liver. This finding i...