منابع مشابه
Protein disulphide-isomerase and the formation of native disulphide bonds.
Disulphide bonds are found in practically every class of extracellular protein, and the formation of disulphide bonds must be regarded as a key post-translational modification of secretory proteins. Despite this, and despite the fact that the existence of disulphide bonds has been known for many years, the mechanism of disulphide bond formation during protein biosynthesis and secretion is not w...
متن کاملSignificance of the disulphide bonds of human growth hormone.
Growth hormone (GH) structure is stabilised by two disulphide bonds, C53-C165 and C182-C189 in human GH. Researchers have investigatedthe role of these structural features since the late 1960s. Early studies implied that the disulphide bonds would not be importantfor biological activity of GH. However, more advanced techniques, as well as clues from patients carrying mutations in their GH1 gene...
متن کاملDifferential reduction of interchain disulphide bonds of mouse immunoglobulin G.
The relative lability of the interchain disulphide bonds of mouse G(2a)-myeloma protein 5563 was studied as a function of 2-mercaptoethanol concentration. Analysis of partial-reduction mixtures by polyacrylamide-gel electrophoresis and microdensitometry showed that the disulphide bonds between light and heavy chains are much more susceptible to reduction than the bonds between heavy chains. At ...
متن کاملRe-formation of disulphide bonds in reduced antithrombin III.
Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 7...
متن کاملDegradation of protein disulphide bonds in dilute alkali.
The degradation of S--S bonds in 0.2 M-NaOH at 25 degrees C was studied for a series of proteins and simple aliphatic disulphide compounds, by using cathodic stripping voltammetry, ion-selective-electrode potentiometry, spectrophotometry and ultrafiltration. The disulphide bonds that dissociated in 0.2 M-NaOH were usually those that are solvent accessible and that can be reduced by mild chemica...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1968
ISSN: 0306-3283
DOI: 10.1042/bj1100036pb