Structure of heavy chain from strain 13 guinea pig immunoglobulin-G(2). II. Amino acid sequence of the carboxyl-terminal and hinge region cyanogen bromide fragments

Kj, Turner; Cebra, J J

doi:10.1021/bi00777a002

Biochemistry

1971

DOI: 10.1021/bi00777a002

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Structure of heavy chain from strain 13 guinea pig immunoglobulin-G(2). II. Amino acid sequence of the carboxyl-terminal and hinge region cyanogen bromide fragments

Turner Kj¹,

J J Cebra²

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Cited by 30 publications

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Comparative studies of sheep immunoglobulins IgG₁ and IgG₂: Amino acid sequence of carboxy‐terminal cyanogen bromide fragments from their heavy chains

1975

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Sheep immunoglobulin IgG1 and immunoglobulin IgG2 heavy chains were treated with cyanogen bromide. The fractions from the C-terminal end of the heavy chains were isolated and purified, and the amino acid sequences gamma1 and gamma2 heavy chains had the identical sequence: Met-His-Glx-Ala-Leu-His-Asx-His-Tyr-Thr-Glx-Lys-Ser-Ile-Ser-Lys-Pro-Pro-Gly. Comparison with the C-terminal peptides of other species, reported in the literature, suggests that the subclasses are the results of recent evolutionary processes. Residues at position 4 from the C-terminus may be phylogenetically related.

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Comparative studies of sheep immunoglobulins IgG₁ and IgG₂: Amino acid sequence of carboxy‐terminal cyanogen bromide fragments from their heavy chains

1975

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Cytophilic activity of enzymatically derived fragments of guinea pig IgG₂

1976

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The hydrolysis products from short term exposure of guinea pig IgG2 to papain and pepsin have been characterized. Papain hydrolysis liberates 4 types of Fc fragment, only one of which retains both an interchain disulfide bond and an intact CH2 domain, cFc, mol.wt. 56 000. The other three fragments noncovalently linked Fc (nFc) (mol.wt. 56 000), incomplete Fc (iFc) (mol.wt. 39 000) and Fc' (23 000) represent further degradation products of covalently linked complete Fc (cFc). The cytophilic activities of these fragments as well as F(ab')2 and pFc' from pepsin hydrolysis, were studied to determine the domain(s) responsible for binding to homologous peritoneal macrophages. Only the native immunoglobulin and the intact cFc manifested cytophilic activity; in particular pepsin-derived pFc' and Fc' were inactive. Following mild reduction and alkylation, performed to affect only the interchain disulfide bonds, the cytophilic activity of cFc was markedly reduced. The low cytophilic activity in the pFc' fragment suggests that the CH2 domains play a major part in binding to the macrophage Fc receptor through a site(s) stabilized by the interchain disulfide bonds.

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Comparison of the cytophilic activities of guinea pig IgG₁ and IgG₂ antibodies

Leslie

Cohen

1976

Eur J Immunol

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Monomeric guinea pig IgGl binds to homologous peritoneal macrophages, though less effectively than IgGz . It binds t o the cells with a lower association constant (K, = 0.61 f 0.22 x lo6 L/M at 20 "C) than IgGz (Ka = 1.44 k 0.16 x lo6 L/M), and the number of IgGI receptor sites per cell (1.3 k 0.18 x l o 6 ) is about one-half that for IgGz (2.65 2 0.45 x lo6). Enhanced IgGl binding is observed on immune complex formation, though the increase in avidity of the complexes is dependent on their size. Marked enhancement of avidity with increase in complex size occurs only with small complexes (containing less than seven antibody molecules): with larger complexes a plateau in avidity appears to be reached. Immune complex binding is inhibited by monomeric IgG,. Comparative studies with IgGl and IgG, demonstrate that IgGl is bound t o the same cell type as IgG, (primarily, the macrophage) by a nonidentical, though related, receptor.

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Structure of heavy chain from strain 13 guinea pig immunoglobulin-G(2). II. Amino acid sequence of the carboxyl-terminal and hinge region cyanogen bromide fragments

Cited by 30 publications

References 30 publications

Comparative studies of sheep immunoglobulins IgG₁ and IgG₂: Amino acid sequence of carboxy‐terminal cyanogen bromide fragments from their heavy chains

Comparative studies of sheep immunoglobulins IgG₁ and IgG₂: Amino acid sequence of carboxy‐terminal cyanogen bromide fragments from their heavy chains

Cytophilic activity of enzymatically derived fragments of guinea pig IgG₂

Comparison of the cytophilic activities of guinea pig IgG₁ and IgG₂ antibodies

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Structure of heavy chain from strain 13 guinea pig immunoglobulin-G(2). II. Amino acid sequence of the carboxyl-terminal and hinge region cyanogen bromide fragments

Cited by 30 publications

References 30 publications

Comparative studies of sheep immunoglobulins IgG1 and IgG2: Amino acid sequence of carboxy‐terminal cyanogen bromide fragments from their heavy chains

Comparative studies of sheep immunoglobulins IgG1 and IgG2: Amino acid sequence of carboxy‐terminal cyanogen bromide fragments from their heavy chains

Cytophilic activity of enzymatically derived fragments of guinea pig IgG2

Comparison of the cytophilic activities of guinea pig IgG1 and IgG2 antibodies

Contact Info

Product

Resources

About

Comparative studies of sheep immunoglobulins IgG₁ and IgG₂: Amino acid sequence of carboxy‐terminal cyanogen bromide fragments from their heavy chains

Comparative studies of sheep immunoglobulins IgG₁ and IgG₂: Amino acid sequence of carboxy‐terminal cyanogen bromide fragments from their heavy chains

Cytophilic activity of enzymatically derived fragments of guinea pig IgG₂

Comparison of the cytophilic activities of guinea pig IgG₁ and IgG₂ antibodies