Disulfide Bonds in Egg-White Riboflavin-Binding
نویسندگان
چکیده
منابع مشابه
The 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 کاملRiboflavin Bound to Egg-White Flavoproteint
The resonance Raman spectra of [2-13C]-, [4a-I3C] -, [4-I3C]-, [ 1 Oa-I3C]-, [2,4,4a, 10a-I3C]-, [ 5-I5N] -, [ 1,3-I5N]-, and [ 1,3,5-'5N]riboflavin bound to egg-white proteins were observed for N(3) -H and N(3)-D forms with spontaneous Raman technique by using the 488.0-nm excitation line of an argon ion laser. The fluorescence of riboflavin was quenched by forming a complex with egg-white rib...
متن کاملFormation 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 binding of flavin derivatives to the riboflavin-binding protein of egg white. A kinetic and thermodynamic study.
A method is described for the preparation and isolation of a riboflavin-binding protein in gram quantity. The product is found to be homogeneous in size and in binding character but slightly heterogeneous in net charge; it consists of a single polypeptide chain of about 30,000 daltons when examined by SDS gel electrophoresis. An affinity chromatography method is described by which flavin analog...
متن کاملProfile of the disulfide bonds in acetylcholinesterase.
The inter- and intrasubunit disulfide bridges for the 11 S form of acetylcholinesterase isolated from Torpedo californica have been identified. Localized within the basal lamina of the synapse, the dimensionally asymmetric forms of acetylcholinesterase contain either two (13 S) or three (17 S) sets of catalytic subunits linked to collagenous and noncollagenous structural subunits. Limited prote...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1982
ISSN: 0014-2956
DOI: 10.1111/j.1432-1033.1982.tb05800.x