Formation of the four isomers of hen egg white lysozyme containing three native disulfide bonds and one open disulfide bond
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چکیده
منابع مشابه
Formation of the four isomers of hen egg white lysozyme containing three negative disulfide bonds and one open disulfide bond.
Reduced partially carboxymethylated hen egg white lysozyme (mucopeptide N-acetylmuramoylhydrolase; EC 3.2.1.17) (approximately 0.8 mol of [1-(14)C]carboxymethyl groups) was air oxidized at pH 8.0 and 37 degrees in the presence of 1.5 mM 2-mercaptoethanol for 36 hr. Gel filtration of this product gave the lower (native) and higher hydrodynamic volume forms, both containing radioactivity (approxi...
متن کاملThe Disulfide Bonds of Egg White Lysozyme (muramidase).
The availability of the amino acid sequence of egg white lysoeyme makes it possible to identify the pairing of the 8 half-cystine residues that give rise to the four disulfide bonds present in the native protein (1,2). In establishing the positions of the disulfide bonds in insulin (3, 4) and ribonuclease (5, 6) it was shown that disulfide interchange, which occurs under certain experimental co...
متن کاملNative disulfide bond formation in proteins.
Native disulfide bond formation is critical for the proper folding of many proteins. Recent studies using newly identified protein oxidants, folding catalysts, and mutant cells provide insight into the mechanism of oxidative protein folding in vivo. This insight promises new strategies for more efficient protein production.
متن کاملHen Egg - white Lysozyme Crystals
Proton tautomerism is a general phenomenon in organic molecules and plays a vital role in many fields of chemistry and biochemistry. The tautomerism of salicylideneanilines [eq(1)] has attracted a considerable attention because it is closely related to thermoand photochromism. Salicylideneanilines greatly favor the enol form over the cis-keto form in the gas phase. We demonstrate here that the ...
متن کاملThe bonds that tie: catalyzed disulfide bond formation.
The pioneering studies of Anfinsen on ribonuclease have guided much of the research in the field of protein folding (Anfinsen et al., 1961). Anfinsen showed that, in vitro, reduced and denatured ribonuclease could refold into active enzyme with the formation of the appropriate disulfide bonds. These findings demonstrated that there was sufficient information in the primary amino acid sequence o...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1977
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.74.6.2362