Preparation and Kinetic Characterization of a Series of βW37 Variants of Human Hemoglobin A:  Evidence for High-Affinity T Quaternary Structures†

Biochemistry ◽  
1998 ◽  
Vol 37 (13) ◽  
pp. 4325-4335 ◽  
Author(s):  
Laura D. Kwiatkowski ◽  
Hilda L. Hui ◽  
Anita Wierzba ◽  
Robert W. Noble ◽  
Roxanne Y. Walder ◽  
...  
Keyword(s):  
Human Hemoglobin ◽  
Kinetic Characterization ◽  
High Affinity ◽  
Hemoglobin A ◽  
Quaternary Structures

Solution1H NMR Characterization of Axial Interactions of the Proximal and Distal His in the Cyanomet Complexes of the Isolated Chains and the 65 kDa Intact Tetramer of Human Hemoglobin A

2001 ◽  
Vol 123 (18) ◽  
pp. 4266-4274 ◽  
Author(s):  
Gerd N. La Mar ◽  
Urszula Kolczak ◽  
Anh-Tuyet T. Tran ◽  
Ellen Y. T. Chien
Keyword(s):  
Human Hemoglobin ◽  
Hemoglobin A ◽  
Nmr Characterization

Isolation and characterization of low and high affinity goat antibodies directed to single antigenic sites on human hemoglobin

1976 ◽  
Vol 13 (11) ◽  
pp. 921-927 ◽  
Author(s):  
Anna L. Tan-Wilson ◽  
Morris Reichlin ◽  
Robert W. Noble
Keyword(s):  
Human Hemoglobin ◽  
High Affinity ◽  
Isolation And Characterization ◽  
Antigenic Sites

scholarly journals Chemical Characterization of Three Hemoglobins G

Blood ◽  
1964 ◽  
Vol 23 (2) ◽  
pp. 193-199 ◽  
Author(s):  
BARBARA H. BOWMAN ◽  
CLARENCE P. OLIVER ◽  
DONALD R. BARNETT ◽  
JAMES E. CUNNINGHAM ◽  
ROSE G. SCHNEIDER
Keyword(s):  
Glutamic Acid ◽  
Electrophoretic Mobility ◽  
Molecular Species ◽  
Tryptic Peptide ◽  
Chemical Characterization ◽  
Human Hemoglobin ◽  
Hemoglobin A ◽  
And Performance ◽  
Β Chain

Abstract Three abnormal hemoglobins identified as G by their electrophoretic mobility and performance on resin chromatography have been discovered in three healthy unrelated Negro individuals in Texas. These three G hemoglobins have been shown to belong to the same molecular species and to have a substitution in the 43rd residue of the β chain. Glutamic acid, which is present in this position in hemoglobin A, has been replaced by alanine in hemoglobin G. According to the recent suggestions on nomenclature of abnormal hemoglobins, hemoglobin GGalveston may be formulated as α24β243 Glu→ ala. Moreover, it has been shown that the following hemoglobins belong to the same molecular species: hemoglobin GGalveston, hemoglobin GPort Arthur, and hemoglobin GTexas. This alteration is the first to be described in the fifth tryptic peptide of the β chain of human hemoglobin and differs from all abnormal hemoglobins previously reported.

scholarly journals Structural and Kinetic Characterization of High-Affinity Lead(II)-Synaptotagmin I Interactions

2018 ◽  
Vol 114 (3) ◽  
pp. 572a
Author(s):  
Sachin Katti ◽  
Bin Her ◽  
Atul Srivastava ◽  
Alexander B. Taylor ◽  
P. John Hart ◽  
...  
Keyword(s):  
Kinetic Characterization ◽  
High Affinity ◽  
Synaptotagmin I

scholarly journals Quaternary Structures of Intermediately Ligated Human Hemoglobin A and Influences from Strong Allosteric Effectors: Resonance Raman Investigation

2005 ◽  
Vol 89 (2) ◽  
pp. 1203-1213 ◽  
Author(s):  
Shigenori Nagatomo ◽  
Masako Nagai ◽  
Yasuhisa Mizutani ◽  
Takashi Yonetani ◽  
Teizo Kitagawa
Keyword(s):  
Resonance Raman ◽  
Human Hemoglobin ◽  
Hemoglobin A ◽  
Allosteric Effectors ◽  
Quaternary Structures

Characterization of Interactions of Nitric Oxide with Human Hemoglobin A by Infrared Spectroscopy

1994 ◽  
Vol 198 (1) ◽  
pp. 281-287 ◽  
Author(s):  
V. Sampath ◽  
X.J. Zhao ◽  
W.S. Caughey
Keyword(s):  
Nitric Oxide ◽  
Infrared Spectroscopy ◽  
Human Hemoglobin ◽  
Hemoglobin A

scholarly journals Kinetic Characterization of a Panel of High-Affinity Monoclonal Antibodies Targeting Ricin and Recombinant Re-Formatting for Biosensor Applications

Antibodies ◽  
2014 ◽  
Vol 3 (2) ◽  
pp. 215-231 ◽  
Author(s):  
Michelle Cummins ◽  
Con Dogovski ◽  
Remy Robert ◽  
Malcolm Alderton ◽  
Damien Chong ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Kinetic Characterization ◽  
High Affinity ◽  
Biosensor Applications

Characterization of a Mode of Specific Binding of Fibrin Monomer through its Amino-Terminal Domain by Macrophages and Macrophage Cell-Lines

1990 ◽  
Vol 63 (02) ◽  
pp. 193-203 ◽  
Author(s):  
John R Shainoff ◽  
Deborah J Stearns ◽  
Patricia M DiBello ◽  
Youko Hishikawa-Itoh
Keyword(s):  
Peritoneal Macrophages ◽  
Affinity Binding ◽  
Macrophage Cell ◽  
High Affinity Binding ◽  
Amino Terminal ◽  
High Affinity ◽  
Terminal Domain ◽  
Weak Binding ◽  
Amino Terminal Domain

SummaryThe studies reported here probe the existence of a receptor-mediated mode of fibrin-binding by macrophages that is associated with the chemical change underlying the fibrinogen-fibrin conversion (the release of fibrinopeptides from the amino-terminal domain) without depending on fibrin-aggregation. The question is pursued by 1) characterization of binding in relation to fibrinopeptide content of both the intact protein and the CNBr-fragment comprising the amino-terminal domain known as the NDSK of the protein, 2) tests of competition for binding sites, and 3) photo-affinity labeling of macrophage surface proteins. The binding of intact monomers of types lacking either fibrinopeptide A alone (α-fibrin) or both fibrinopeptides A and B (αβ-fibrin) by peritoneal macrophages is characterized as proceeding through both a fibrin-specific low density/high affinity (BMAX ≃ 200–800 molecules/cell, KD ≃ 10−12 M) interaction that is not duplicated with fibrinogen, and a non-specific high density/low affinity (BMAX ≥ 105 molecules/cell, KD ≥ 10−6 M) interaction equivalent to the weak binding of fibrinogen. Similar binding characteristics are displayed by monocyte/macrophage cell lines (J774A.1 and U937) as well as peritoneal macrophages towards the NDSK preparations of these proteins, except for a slightly weaker (KD ≃ 10−10 M) high-affinity binding. The high affinity binding of intact monomer is inhibitable by fibrin-NDSK, but not fibrinogen-NDSK. This binding appears principally dependent on release of fibrinopeptide-A, because a species of fibrin (β-fibrin) lacking fibrinopeptide-B alone undergoes only weak binding similar to that of fibrinogen. Synthetic Gly-Pro-Arg and Gly-His-Arg-Pro corresponding to the N-termini of to the α- and the β-chains of fibrin both inhibit the high affinity binding of the fibrin-NDSKs, and the cell-adhesion peptide Arg-Gly-Asp does not. Photoaffinity-labeling experiments indicate that polypeptides with elec-trophoretically estimated masses of 124 and 187 kDa are the principal membrane components associated with specifically bound fibrin-NDSK. The binding could not be up-regulated with either phorbol myristyl acetate, interferon gamma or ADP, but was abolished by EDTA and by lipopolysaccharide. Because of the low BMAX, it is suggested that the high-affinity mode of binding characterized here would be too limited to function by itself in scavenging much fibrin, but may act cooperatively with other, less limited modes of fibrin binding.

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