# Evidence for a C-terminal tyrosine residue in human and mouse B-lymphocyte membrane μ chains

@article{Mcilhinney1978EvidenceFA,
title={Evidence for a C-terminal tyrosine residue in human and mouse B-lymphocyte membrane $\mu$ chains},
author={R. A. J. Mcilhinney and Neil E. Richardson and Arnold Feinstein},
journal={Nature},
year={1978},
volume={272},
pages={555-557}
}
• Published 1978
• Chemistry, Medicine
• Nature
THE antigen receptor on the plasma membrane of both human and murine bone marrow-derived (B) lymphocytes has been shown to be mainly monomeric IgM (refs 1–5), but the mechanism of attachment of this IgM is not known. Studies on other membrane proteins (for example, glycophorin6, cytochrome b5, (ref. 7) and probably HLA8) have shown that they are bound to the membrane by means of a hydrophobic polypeptide stretch in the C-terminal region, but secreted IgM heavy chains terminate in an extra… Expand
24 Citations
The immunoglobulin μ chains of membrane-bound and secreted IgM molecules differ in their C-terminal segments
This study compares the structures of the secreted and membrane-bound mu (micron) heavy chains by peptide mapping, micro-sequence and carboxypeptidase analyses, and suggests that the micron and microsecond chains from a given B cell are identical except for their 41 and 20 residue C-terminal segments, respectively. Expand
A major structural difference between membrane‐bound and secreted IgM of normal mouse spleen cells is located in the C‐terminal region of their heavy chains
• Chemistry, Medicine
• FEBS letters
• 1980
It is shown that /.I~, but not ps chains, bind detergents, thus suggesting the presence of an hydrophobic region in the molecule, and structural differences are shown, at least in part, located towards the C-terminal end of the or chains. Expand
Biosynthesis and structure of membrane and secretory immunoglobulins
• Biology, Medicine
• Molecular and Cellular Biochemistry
• 2004
Evidence is accumulating that all membrane-bound Ig heavy chain classes may contain similar hydrophobic structures necessary for anchorage of the molecules into the lipid bilayer. Expand
Synthesis of secreted and membrane-bound immunoglobulin mu heavy chains is directed by mRNAs that differ at their 3′ ends
It was shown that the 3′ ends of the two μ mRNAs do not cross-hybridize, and apparently two separate 3′ terminal sequences for μ mRNA are encoded in the genome, one that specifies an amino acid sequence appropriate for membrane-binding and a second that is involved in secretion. Expand
Different species of messenger RNA encode receptor and secretory IgM μ chains differing at their carboxy termini
• Biology, Medicine
• Nature
• 1980
It is proposed that the synthetic pathways for receptor and secretory IgM diverge at the post-transcriptional level, possibly by differential RNA splicing to give mRNA molecules with or without a translatable ‘tail’ segment. Expand
B lymphocytes contain three species of μ chains
• Biology
• 1978
The murine B cell line cloned from a single cell, 38C‐13, synthesizes three species of μ chains, that of cell surface membrane IgM (m‐μ), that of secreted IgM (s‐μ) and that of intracellular IgMExpand
The monomeric IgM and IgD molecules on the cell surface of B lymphocytes are generally thought to be integral membrane antigen receptors
The monomeric IgM and IgD molecules on the cell surface of B lymphocytes are generally thought to be integral membrane antigen receptors (1-3). These molecules are believed to be involved inExpand
Chemical characterisation of the Fab and Fc fragments from surface immunoglobulin
• Chemistry, Medicine
• Nature
• 1980
The results confirm the observation that sIg is a hydrophobic protein which binds detergent15–17, and demonstrate that the site of detergent binding is located in the C-terminal portion of the sIG heavy chain. Expand
Immunoglobulin messenger RNAs in murine cell lines that have characteristics of immature B lymphocytes
• Medicine, Biology
• Cell
• 1979
Abstract The immunoglobulin-encoding messenger RNAs in a pre-B cell-like lymphoma line, 70Z/3, were characterized according to size, concentration in nuclear and cytoplasmic compartments and responseExpand
Interactions of gamma-immunoglobulins with lipid mono- or bilayers and liposomes. Existence of two conformations of gamma-immunoglobulins of different hydrophobicities.
• Chemistry, Medicine
• Molecular immunology
• 1981
The possible existence of two Ig isomers is discussed in relation to the mechanism of γ-immunoglobulin passage through the endoplasmic membrane and fixation into the plasma membrane. Expand

#### References

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• Medicine, Chemistry
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Comparison of tryptic peptide maps of the immunoglobulin M µ chains with two other mouse µ chains showed a large number of common peptides but the same degree of variability in the remaining peptides as seen in γ and α heavy chains. Expand
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Results are presented which indicate that actin, or a protein exhibiting a high degree of homology withActin, is a major component of extensively purified lymphocyte plasma membrane from pig and human sources. Expand
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A species of cytochrome b(5) with a monomer molecular weight of 16,700 has been isolated from rabbit-liver microsomes by a procedure that uses detergents and avoids the use of any proteolytic or lipolytic enzymes, and appears to contain an extremely hydrophobic appendage of 40 amino acids at the N-terminus. Expand
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The homology of the constant regions of immunoglobulin �, γ, α, and ε heavy chains reveals evolutionary relationships and suggests that two genes code for each heavy chain. Expand