The Amino Acid Sequence of the Fc Fragment of Rabbit Immunoglobulin G [PDF]
Journal of Biological Chemistry, 1968 Reaction of S-carboxymethyl-Fc fragment from rabbit immunoglobulin G with cyanogen bromide cleaves the fragment into five unique peptides, each of which has been isolated by chromatographic methods. The amino acid composition of the five peptides accounts closely for the amino acid composition of the Fc fragment.
Robert Delaney, Robert L. Hill
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Reversible Dissociation of Fragment Fc of Rabbit γG-Immunoglobulin
Journal of Biological Chemistry, 1966 Abstract Crystallized Fragment Fc of rabbit γG-globulin, prepared by digestion with papain in the presence of 0.05 m l-cysteine, dissociates into half-fragments in 0.05 m NaCl at pH 2.7. Dissociation is approximately half-complete at pH 3.1. The conditions are similar to those required for dissociation of γG-globulin into half-molecules, which supports
F. P. Inman, Alfred Nisonoff
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Enzymic degradation of the Fc fragment of rabbit immunoglobulin IgG [PDF]
Biochemical Journal, 1967 The digestion of the Fc fragment of rabbit immunoglobulin IgG by several proteolytic enzymes was investigated by using gel filtration and starch-gel electrophoresis in 8m-urea-formate as criteria of the extent of degradation. Though fragment Fc and mildly reduced fragment Fc proved resistant to tryptic hydrolysis, papain and pepsin cleaved the fragment
Prahl Jw
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13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G [PDF]
, 1993 The mode of interaction of the B domain (FB) of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G (IgG) has been investigated by 13C NMR spectroscopy.
Koichi Kato +5 more
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Subfragments from the Fc fragment of human immunoglobulin G. Isolation and physicochemical characterization [PDF]
Biochemical Journal, 1968 A fragment termed fragment Fc′ and a related fragment termed fragment pFc′ produced by the actions of papain and pepsin respectively on human immunoglobulin G have been isolated and characterized. Amino acid analyses and experiments utilizing cyanogen bromide to cleave the methionyl bonds of the Fc′ and pFc′ fragments make it possible to locate both ...
Malcolm Turner, H. Bennich
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Chloroplast transformation for bioencapsulation and oral delivery using the immunoglobulin G fragment crystallizable (Fc) domain [PDF]
Scientific Reports, 2023 AbstractProinsulin Like Growth Factor I (prolGF-I) and myostatin (Mstn) regulate muscle regeneration and mass when intravenously delivered. We tested if chloroplast bioencapsulated forms of these proteins may serve as a non-invasive means of drug delivery through the digestive system.
Lisa M. LaManna +4 more
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Structure analysis of goose immunoglobulin Y Fc fragment [PDF]
Central European Journal of Immunology, 2013 Objective: Goose immunoglobulin Y (IgY)-Fc fragment gene is cloned. Material and methods: In order to obtain a certain length (106 bp) of constant domain gene, a pair of primer was designed according to the conserved nucleotide sequence of duck (CAA46322) and chick en (S00390) IgY-Fc fragment that was published by the GenBank.
Lei Jiang +4 more
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Intrachain disulphide bridges in immunoglobulin G heavy chains. The Fc fragment [PDF]
Biochemical Journal, 1968 The disulphide bridges of the Fc fragment (C-terminal half of the heavy chain) have been studied in several human immunoglobulins, containing heavy chains of different antigenic types (γ1, γ2, γ3 and γ4), and in heavy-chain-disease proteins. Two intrachain disulphide bridges were found to be present.
Blas Frangione +2 more
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Studies on the immunoglobulin-G Fc-fragment receptor from neonatal rat small intestine [PDF]
Biochemical Journal, 1980 1. A method for preparing the small-intestinal brush-border membrane of neonatal rats is described in which enzymic methods are used to remove associated polysaccharide and cell nuclei. 2. 125I-labelled IgG (immunoglobulin G) and 125I-labelled IgG Fc fragment have high specific binding and low non-specific binding to brush borders prepared in this way.
Kristin Wallace, Anthony R. Rees
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The interaction between protein A and immunoglobulin G as studied with the Fc‐fragment of a myeloma protein by circular dichroism [PDF]
FEBS Letters, 1975 Protein A is a cell-wall constituent from Staphylococcus UUI~W [ 1,2] with the ability to react with nonimmune immunoglobulins from several mammalia [3,4]. The active binding site for protein A is situated in the Fc-region of human IgCl, IgG2 and IgG4 [ 561. As a consequence of the reaction, the complement system, for instance, is activated, as well as
Ingvar Sjöholm
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