scholarly journals Anti-phosphocholine hybridoma antibodies. I. Direct evidence for three distinct families of antibodies in the murine response

1981 ◽  
Vol 153 (2) ◽  
pp. 352-364 ◽  
Author(s):  
JL Claflin ◽  
S Hudak ◽  
A Maddalena
Keyword(s):  
Binding Site ◽  
Isoelectric Focusing ◽  
Direct Evidence ◽  
Structural Characteristics ◽  
Site Specificity ◽  
The Third ◽  
Myeloma Proteins ◽  
Remarkable Degree ◽  
Serological Studies

Biochemical and serological studies were performed on more than 400 anti- phosphocholine (PC) hybridoma proteins (HP) derived from six strains of mice; 26 of these HP were examined in detail. All HP possessed specificity for PC, and all those tested contained an H-chain idiotypic determinant, V(H)-PC, which is shared by PC-binding myeloma proteins (BMP) and anti-PC antibodies. Among the HP, three well-defined and distinct families that correlated well with previous studies on serum anti-PC antibodies were identified. The largest group shared idotypic determinants, an L-chain isoelectric focusing (IEF) pattern, and a binding site specificity with the PC-BMP, T15. Using the same criteria, a second group was found to be strikingly similar to another PC-BMP, M603. The third group possessed an idiotypic determinant and an L-chain IEF profile similar to M511, but differences in binding site specificities were observed among the HP. The latter two groups contained members whose L-chain IEF profiles were not identical to other members of that group. Thus, among strains there is a remarkable degree of conservation among responding anti-PC antibodies, in both the kinds of anti-PC families that exist and the immunochemical and structural characteristics of various members within a family. Differences in at least one parameter were observed in each family, demonstrating that even a relatively restricted response is heterogeneous. However, this diversity seems to operate within certain constraints.

scholarly journals A discontinuous factor H binding site in the third component of complement as delineated by synthetic peptides.

1988 ◽  
Vol 263 (24) ◽  
pp. 12147-12150 ◽  
Author(s):  
J D Lambris ◽  
D Avila ◽  
J D Becherer ◽  
H J Müller-Eberhard
Keyword(s):  
Binding Site ◽  
Synthetic Peptides ◽  
Factor H ◽  
The Third ◽  
Third Component Of Complement

scholarly journals Conversion of MyoD to a Neurogenic Factor: Binding Site Specificity Determines Lineage

Cell Reports ◽  
2015 ◽  
Vol 10 (12) ◽  
pp. 1937-1946 ◽  
Author(s):  
Abraham P. Fong ◽  
Zizhen Yao ◽  
Jun Wen Zhong ◽  
Nathan M. Johnson ◽  
Gist H. Farr ◽  
...  
Keyword(s):  
Binding Site ◽  
Site Specificity ◽  
Factor Binding Site ◽  
Factor Binding ◽  
Neurogenic Factor

Dominant Thermodynamic Role of the Third Independent Receptor Binding Site in the Receptor-Associated Protein RAP†

Biochemistry ◽  
2001 ◽  
Vol 40 (50) ◽  
pp. 15408-15417 ◽  
Author(s):  
Olav M. Andersen ◽  
Frederick P. Schwarz ◽  
Edward Eisenstein ◽  
Christian Jacobsen ◽  
Søren K. Moestrup ◽  
...  
Keyword(s):  
Binding Site ◽  
Receptor Binding ◽  
Receptor Binding Site ◽  
Receptor Associated Protein ◽  
The Third

Microheterogeneity and sialic acid in human plasma angiotensinogens in various physiological states

1978 ◽  
Vol 56 (9) ◽  
pp. 892-899 ◽  
Author(s):  
A. A. Faiers ◽  
A. Y. Loh ◽  
D. H. Osmond
Keyword(s):  
Sialic Acid ◽  
Rat Liver ◽  
Isoelectric Focusing ◽  
Structural Characteristics ◽  
Gel Filtration ◽  
Angiotensin I ◽  
Third Trimester ◽  
Human Renin ◽  
Isoelectric Ph ◽  
Normal Men

Pooled or individual plasmas from normal men, women, pregnant women (third trimester), anephric women, and rat liver perfusates were used as sources of angiotensinogen. The plasmas were fractionated and desalted by Sephadex gel filtration, then subjected to isoelectric focusing in a pH 4 to 6 gradient on 40 × 4 cm slabs of polyacrylamide gel. The gels were cut transversely into 0.5-cm-wide strips, the pH measured, and their angiotensinogen concentrations determined by incubation with excess human renin and radioimmunoassay of the product, angiotensin I. This revealed several peaks of angiotensinogen concentration indicative of microheterogeneity in all cases. Contrary to other claims, the isoelectric pH profiles of angiotensinogens in the various physiological states were substantially alike. Major peaks were found at pH 4.75 to 4.85 and 4.9 to 5.0 and minor peaks at pH 4.5 to 4.7 and 5.0 to 5.2; this resolution was greater than that achieved with rat liver angiotensinogens. Incubation of human angiotensinogens with neuraminidase for 3 or 16 h raised their isoelectric pH by about 0.5 U, probably due to removal of sialic acid. Since microheterogeneity persisted after desialylation, it is probably determined by structural characteristics other than sialic acid composition.

scholarly journals RUNX1 regulates site specificity of DNA demethylation by recruitment of DNA demethylation machineries in hematopoietic cells

2017 ◽  
Vol 1 (20) ◽  
pp. 1699-1711 ◽  
Author(s):  
Takahiro Suzuki ◽  
Yuri Shimizu ◽  
Erina Furuhata ◽  
Shiori Maeda ◽  
Mami Kishima ◽  
...  
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Ectopic Expression ◽  
Hematopoietic Cells ◽  
Dna Demethylation ◽  
Site Specificity ◽  
Gene Promoters ◽  
Hematopoietic Development ◽  
Key Points

Key PointsEctopic expression of RUNX1 induces binding site–directed DNA demethylation, in which hematopoietic gene promoters are included. RUNX1 binding sites are enriched in demethylated regions during hematopoietic development.

Isolation and Identification of Poplar Isoplastocyanins

2010 ◽  
Vol 65 (3-4) ◽  
pp. 225-230 ◽  
Author(s):  
Mitko I. Dimitrov ◽  
Anthony A. Donchev ◽  
Alexandra C. Shosheva ◽  
Vladimir I. Getov ◽  
Nedyalka P. Terezova ◽  
...  
Keyword(s):  
Isoelectric Focusing ◽  
Physiological Significance ◽  
Purification Procedure ◽  
Isolation And Identification ◽  
Isolation And Purification ◽  
The Third ◽  
Present Procedure ◽  
Vis Spectroscopy ◽  
Isoelectric Points

An improved four-stage isolation and purification procedure for preparing poplar isoplastocyanins is described in detail. Absorbance (UV-VIS) spectroscopy and isoelectric focusing (IEF) are used to determine the protein purity and identity. The present procedure increases twice the total plastocyanin (PC) yield. Four PC isoform fractions are consecutively isolated at the third chromatographic step: oxidized PCa(II) and PCb(II) and reduced PCb(I) and PCa(I). PCa(II) and PCb(II) obtained at the fourth chromatographic step are highly purified PC isoforms which show the purity index (p.i.) A278/A597 ≤ 0.85. Isoelectric points (pI values) of the PC isoforms are found to be at pH 3.92 ± 0.04 for PCa and at pH 3.85 ± 0.02 for PCb. The results of appropriate biological experiments that include the highly purified poplar PC isoforms could give answers to the questions about the physiological significance of PC dimorphism for photosynthesis.

Conformational changes in the third PDZ domain of the neuronal postsynaptic density protein 95

2019 ◽  
Vol 75 (4) ◽  
pp. 381-391 ◽  
Author(s):  
Ana Camara-Artigas ◽  
Javier Murciano-Calles ◽  
Jose C. Martínez
Keyword(s):  
Binding Site ◽  
Conformational Changes ◽  
Pdz Domain ◽  
Postsynaptic Density ◽  
Crystal Form ◽  
Space Groups ◽  
The Third ◽  
Conformational Plasticity ◽  
Α Helix ◽  
Postsynaptic Density Protein

PDZ domains are protein–protein recognition modules that interact with other proteins through short sequences at the carboxyl terminus. These domains are structurally characterized by a conserved fold composed of six β-strands and two α-helices. The third PDZ domain of the neuronal postsynaptic density protein 95 has an additional α-helix (α3), the role of which is not well known. In previous structures, a succinimide was identified in the β2–β3 loop instead of Asp332. The presence of this modified residue results in conformational changes in α3. In this work, crystallographic structures of the following have been solved: a truncated form of the third PDZ domain of the neuronal postsynaptic density protein 95 from which α3 has been removed, D332P and D332G variants of the protein, and a new crystal form of this domain showing the binding of Asp332 to the carboxylate-binding site of a symmetry-related molecule. Crystals of the wild type and variants were obtained in different space groups, which reflects the conformational plasticity of the domain. Indeed, the overall analysis of these structures suggests that the conformation of the β2–β3 loop is correlated with the fold acquired by α3. The alternate conformation of the β2–β3 loop affects the electrostatics of the carboxylate-binding site and might modulate the binding of different PDZ-binding motifs.

Defining a second epitope for heparin-induced thrombocytopenia/thrombosis antibodies using KKO, a murine HIT-like monoclonal antibody

Blood ◽  
2002 ◽  
Vol 99 (4) ◽  
pp. 1230-1236 ◽  
Author(s):  
Zhong Q. Li ◽  
Weiyi Liu ◽  
Kwang S. Park ◽  
Brue S. Sachais ◽  
Gowthani M. Arepally ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Binding Site ◽  
Binding Sites ◽  
Heparin Therapy ◽  
Common Complication ◽  
Platelet Factor ◽  
Heparin Induced Thrombocytopenia ◽  
The Third ◽  
N Terminus ◽  
A Site

Heparin-induced thrombocytopenia/thrombosis (HIT/T) is a common complication of heparin therapy that is caused by antibodies to platelet factor 4 (PF4) complexed with heparin. The immune response is polyclonal and polyspecific, ie, more than one neoepitope on PF4 is recognized by HIT/T antibodies. One such epitope has been previously identified; it involves the domain between the third and fourth cysteine residues in PF4 (site 1). However, the binding sites for other HIT/T antibodies remain to be defined. To explore this issue, the binding site of KKO, an HIT/T-like murine monoclonal antibody, was defined. KKO shares a binding site with many HIT/T antibodies on PF4/heparin, but does not bind to site 1 or recognize mouse PF4/heparin. Therefore, the binding of KKO to a series of mouse/human PF4 chimeras complexed with heparin was examined. KKO recognizes a site that requires both the N terminus of PF4 and Pro34, which immediately precedes the third cysteine. Both regions lie on the surface of the PF4 tetramer in sufficient proximity (within 0.74 nm) to form a contiguous antigenic determinant. The 10 of 14 HIT/T sera that require the N terminus of PF4 for antigen recognition also require Pro34 to bind. This epitope, termed site 2, lies adjacent to site 1 in the crystal structure of the PF4 tetramer. Yet sites 1 and 2 can be recognized by distinct populations of antibodies. These studies further help to define a portion of the PF4 tetramer to which self-reactive antibodies develop in patients exposed to heparin.

Pulmonary arterial thrombosis in a neonate with homozygous deficiency of antithrombin III: successful outcome following pulmonary thrombectomy and infusions of antithrombin III concentrate

2000 ◽  
Vol 10 (3) ◽  
pp. 275-278 ◽  
Author(s):  
K. Roman ◽  
E. Rosenthal ◽  
R. Razavi
Keyword(s):  
Binding Site ◽  
Arterial Thrombosis ◽  
Antithrombin Iii ◽  
Pulmonary Trunk ◽  
Successful Outcome ◽  
Heparin Binding ◽  
The Third ◽  
Heparin Binding Site ◽  
Surgical Thrombectomy ◽  
Pulmonary Arterial

AbstractWe report a newborn male who presented with severe central cyanosis on the third day of life. Partial thrombotic obstruction of the pulmonary trunk secondary to Antithrombin III (homozygous defect of heparin binding site) deficiency was subsequently diagnosed. Surgical thrombectomy, and infusions of Antithrombin III concentrate, led to a successful outcome. We postulate that intrauterine thrombosis occurred to give this unusual presentation.

Sign in / Sign up

Export Citation Format

Share Document