Carboxy-terminal structure of the α chain of human IgA [immunoglobulin A] myeloma proteins

Biochemistry ◽  
1971 ◽  
Vol 10 (10) ◽  
pp. 1808-1812 ◽  
Author(s):  
James W. Prahl ◽  
Carlos A. Abel ◽  
Howard M. Grey
Keyword(s):  
Immunoglobulin A ◽  
Myeloma Proteins ◽  
Α Chain ◽  
Terminal Structure ◽  
Carboxy Terminal

Structure of immunoglobulin A. Cysteine-containing peptides of the α chain of an immunoglobulin A1 myeloma protein

Biochemistry ◽  
1973 ◽  
Vol 12 (25) ◽  
pp. 5186-5194 ◽  
Author(s):  
Enrique Mendez ◽  
Blas Frangione ◽  
Edward C. Franklin
Keyword(s):  
Immunoglobulin A ◽  
Myeloma Protein ◽  
Α Chain

scholarly journals ADP-induced platelet aggregation depends on the conformation or availability of the terminal gamma chain sequence of fibrinogen. Study of the reactivity of fibrinogen Paris 1

Blood ◽  
1987 ◽  
Vol 70 (2) ◽  
pp. 558-563 ◽  
Author(s):  
MH Denninger ◽  
M Jandrot-Perrus ◽  
J Elion ◽  
O Bertrand ◽  
GA Homandberg ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
High Performance ◽  
Cross Linking ◽  
Gamma Chain ◽  
Carboxy Terminal Region ◽  
Chain Polymerization ◽  
Triethylene Tetramine ◽  
Terminal Structure ◽  
Carboxy Terminal ◽  
Peptide Insertion

Abstract Fibrinogen Paris I contains a mutant gamma chain that is longer than the normal chain, resulting in altered fibrin polymerization and cross- linking. Because these functions involve the carboxy-terminal region of the gamma chain, we decided to determine whether fibrinogen Paris I or the isolated Paris I gamma chain supports normal ADP-induced platelet aggregation, a function that requires the ultimate 12 residues of the normal gamma chain (400 through 411). Aggregation of ADP-stimulated normal platelets was defective with fibrinogen Paris I and markedly depressed with the gamma Paris I chain. These findings prompted us to characterize the carboxy-terminal structure of the region of the gamma Paris I chain responsible for this activity. The carboxy-terminal cyanogen bromide (CNBr) peptide of the normal gamma chain (385 through 411) or that from gamma Paris I was isolated by differential adsorption to triethylene-tetramine resin or by reverse-phase high-performance liquid chromatography (HPLC). The CNBr peptide from the Paris I gamma chain was identical to that of the normal gamma chain in its retention time on HPLC, its amino acid composition, and its sequence. Thus, the primary structure of the gamma Paris I chain from residue 384 through 411 is normal, indicating that a peptide insertion has occurred upstream from residue 384, resulting in an impairment of those physiologic functions attributable to the carboxy-terminal end of the gamma chain from position 384 (ie, cross-linking, ADP-induced platelet aggregation, and at least a portion of the gamma chain polymerization site). These observations demonstrate that the gamma chain platelet recognition site in the fibrinogen molecule is necessary but not alone sufficient to support normal ADP-induced platelet aggregation. There appears to be an additional requirement for normal conformation of the gamma chain or availability of its terminal sequence during the interaction of fibrinogen with platelets.

Correction - Spectral Changes on Binding of Oligosaccharides to Murine Immunoglobulin A Myeloma Proteins

Biochemistry ◽  
1973 ◽  
Vol 12 (25) ◽  
pp. 5224-5224
Author(s):  
M. Jolley ◽  
S. Rudikoff ◽  
Michael Potter ◽  
C. P. Glaudermans
Keyword(s):  
Immunoglobulin A ◽  
Spectral Changes ◽  
Myeloma Proteins

Characterization of a disulfide bridge linking the J chain to the α chain of polymeric immunoglobulin A

1973 ◽  
Vol 55 (4) ◽  
pp. 1291-1297 ◽  
Author(s):  
Enrique Mendez ◽  
Frances Prelli ◽  
Blas Frangione ◽  
Edward C. Franklin
Keyword(s):  
Immunoglobulin A ◽  
Disulfide Bridge ◽  
J Chain ◽  
Α Chain

Spectral changes on binding of oligosaccharides to murine immunoglobulin A myeloma proteins

Biochemistry ◽  
1973 ◽  
Vol 12 (16) ◽  
pp. 3039-3044 ◽  
Author(s):  
M. E. Jolley ◽  
S. Rudikoff ◽  
Michael Potter ◽  
C. P. J. Glaudemans
Keyword(s):  
Immunoglobulin A ◽  
Spectral Changes ◽  
Myeloma Proteins

scholarly journals Trivalent Vaccine against Botulinum Toxin Serotypes A, B, and E That Can Be Administered by the Mucosal Route

2007 ◽  
Vol 75 (6) ◽  
pp. 3043-3054 ◽  
Author(s):  
Easwaran Ravichandran ◽  
Fetweh H. Al-Saleem ◽  
Denise M. Ancharski ◽  
Mohammad D. Elias ◽  
Ajay K. Singh ◽  
...  
Keyword(s):  
Botulinum Toxin ◽  
Immunoglobulin A ◽  
Mucosal Vaccine ◽  
Human Illness ◽  
Epithelial Barriers ◽  
High Level ◽  
Carboxy Terminal ◽  
Trivalent Vaccine

ABSTRACT Most reports dealing with vaccines against botulinum toxin have focused on the injection route of administration. This is unfortunate, because a mucosal vaccine is likely to be more efficacious for patients and pose fewer risks to health care workers and to the environment. Therefore, efforts were made to generate a mucosal vaccine that provides protection against the botulinum serotypes that typically cause human illness (serotypes A, B, and E). This work demonstrated that carboxy-terminal peptides derived from each of the three serotypes were able to bind to and penetrate human epithelial barriers in vitro, and there was no cross inhibition of membrane binding and transcytosis. The three polypeptides were then tested in vivo as a trivalent vaccine that could be administered to mice by the intranasal route. The results indicated that the mucosal vaccine evoked high secretory titers of immunoglobulin A (IgA), as well as high circulating titers of IgG and IgA, and it also evoked a high level of resistance to challenge with toxin. The immunoglobulin responses and the levels of resistance to challenge were increased by coadministration of adjuvants, such as chitosan and vitamin E. At least three mechanisms were identified to account for the antibody-induced resistance: (i) blockade of toxin absorption across epithelial cells, (ii) enhanced clearance of toxin from the circulation, and (iii) blockade of toxin action at the neuromuscular junction. These results are a compelling demonstration that a mucosal vaccine against multiple serotypes of botulinum toxin has been identified.

051 Carboxy-terminal structure of plectin-2

1997 ◽  
Vol 15 (2) ◽  
pp. 111
Author(s):  
S. Fujiwara ◽  
N. Takeo
Keyword(s):  
Terminal Structure ◽  
Carboxy Terminal

scholarly journals ADP-induced platelet aggregation depends on the conformation or availability of the terminal gamma chain sequence of fibrinogen. Study of the reactivity of fibrinogen Paris 1

Blood ◽  
1987 ◽  
Vol 70 (2) ◽  
pp. 558-563
Author(s):  
MH Denninger ◽  
M Jandrot-Perrus ◽  
J Elion ◽  
O Bertrand ◽  
GA Homandberg ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
High Performance ◽  
Cross Linking ◽  
Gamma Chain ◽  
Carboxy Terminal Region ◽  
Chain Polymerization ◽  
Triethylene Tetramine ◽  
Terminal Structure ◽  
Carboxy Terminal ◽  
Peptide Insertion

Fibrinogen Paris I contains a mutant gamma chain that is longer than the normal chain, resulting in altered fibrin polymerization and cross- linking. Because these functions involve the carboxy-terminal region of the gamma chain, we decided to determine whether fibrinogen Paris I or the isolated Paris I gamma chain supports normal ADP-induced platelet aggregation, a function that requires the ultimate 12 residues of the normal gamma chain (400 through 411). Aggregation of ADP-stimulated normal platelets was defective with fibrinogen Paris I and markedly depressed with the gamma Paris I chain. These findings prompted us to characterize the carboxy-terminal structure of the region of the gamma Paris I chain responsible for this activity. The carboxy-terminal cyanogen bromide (CNBr) peptide of the normal gamma chain (385 through 411) or that from gamma Paris I was isolated by differential adsorption to triethylene-tetramine resin or by reverse-phase high-performance liquid chromatography (HPLC). The CNBr peptide from the Paris I gamma chain was identical to that of the normal gamma chain in its retention time on HPLC, its amino acid composition, and its sequence. Thus, the primary structure of the gamma Paris I chain from residue 384 through 411 is normal, indicating that a peptide insertion has occurred upstream from residue 384, resulting in an impairment of those physiologic functions attributable to the carboxy-terminal end of the gamma chain from position 384 (ie, cross-linking, ADP-induced platelet aggregation, and at least a portion of the gamma chain polymerization site). These observations demonstrate that the gamma chain platelet recognition site in the fibrinogen molecule is necessary but not alone sufficient to support normal ADP-induced platelet aggregation. There appears to be an additional requirement for normal conformation of the gamma chain or availability of its terminal sequence during the interaction of fibrinogen with platelets.

scholarly journals Comparison of the dimensions of the combining sites of the dinitrophenyl-binding immunoglobulin A myeloma proteins MOPC 315, MOPC 460 and XRPC 25 by spin-label mapping

1977 ◽  
Vol 165 (2) ◽  
pp. 199-206 ◽  
Author(s):  
Keith J. Willan ◽  
Derek Marsh ◽  
Christopher A. Sunderland ◽  
Brian J. Sutton ◽  
Simon Wain-Hobson ◽  
...  
Keyword(s):  
Binding Sites ◽  
Immunoglobulin A ◽  
Binding Activity ◽  
The Other ◽  
Spin Labels ◽  
Metal Site ◽  
Myeloma Proteins ◽  
Spin Resonance ◽  
Mouse Immunoglobulin ◽  
Positively Charged

The mouse immunoglobulin A myeloma proteins MOPC 315, MOPC 460 and XRPC 25 all possess dinitrophenyl (Dnp)-binding activity. Differences in specificities were shown by measuring the affinities of a variety of haptens. By using a series of Dnp-spin-labelled haptens, the dimensions of the binding sites of the three myeloma proteins were compared by the method described for protein MOPC 315 [Sutton, Gettins, Givol, Marsh, Wain-Hobson, Willan & Dwek (1977) Biochem. J.165, 177–197]. The dinitrophenyl ring is rigidly held in all three sites. The depths of the sites are all 1.1–1.2nm, but there are differences in the lateral dimensions at the entrance to the sites. For protein XRPC 25 these dimensions are 0.75nm×0.8nm, which may be compared with 0.85nm×1.1nm for protein MOPC 315 and ≥1.0nm×1.1nm for protein MOPC 460. The site in protein MOPC 460 is more symmetrical with respect to the plane of the dinitrophenyl ring than in either of the other two myeloma proteins and also allows greater penetration of solvent. In protein XRPC 25 a positively charged residue was located at the entrance to the site, similarly positioned to that reported for protein MOPC 315 [Sutton, Gettins, Givol, Marsh, Wain-Hobson, Willan & Dwek (1977) Biochem. J.165, 177–197]. All three proteins possess lanthanide-binding sites, but only in protein MOPC 315 is there antagonism between lanthanide and hapten binding. However, the effects of the diamagnetic La(III) on the electron-spin-resonance spectra of bound Dnp spin labels in both proteins MOPC 460 and XRPC 25 suggest an interaction between the two sites. Comparison of this effect with that caused by the addition of the paramagnetic Gd(III) enables the distance between the lanthanide- and hapten-binding sites to be calculated. In both proteins MOPC 460 and MOPC 315 the metal site is approx. 1.0nm from the nitroxide moiety of the spin-labelled hapten, but in protein XRPC 25 this distance is at least 2.0nm.

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