Characterization of new amino-terminal blocking groups in the normal human adult hemoglobin Hb A1b

1995 ◽  
Vol 1 (1) ◽  
pp. 195
Author(s):  
Danielle Promé ◽  
Jean- Claude Promé ◽  
Yves Bloquit ◽  
Jean Rosa
Keyword(s):  
Amino Terminal ◽  
Human Adult ◽  
Normal Human ◽  
Adult Hemoglobin

scholarly journals Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography

2010 ◽  
Vol 66 (11) ◽  
pp. 1144-1152 ◽  
Author(s):  
Andrey Kovalevsky ◽  
Toshiyuki Chatake ◽  
Naoya Shibayama ◽  
Sam-Yong Park ◽  
Takuya Ishikawa ◽  
...  
Keyword(s):  
Protein Crystallography ◽  
Human Adult ◽  
Normal Human ◽  
Adult Hemoglobin ◽  
Neutron Protein Crystallography ◽  
Key Residues

Acrylamide-Gel Electrophoresis of Hemoglobins

1963 ◽  
Vol 9 (2) ◽  
pp. 135-145 ◽  
Author(s):  
Masumi Nakamichi ◽  
Samuel Raymond
Keyword(s):  
Gel Electrophoresis ◽  
Minor Component ◽  
Red Cells ◽  
Minor Components ◽  
Human Adult ◽  
Normal Human ◽  
Adult Hemoglobin ◽  
Hemoglobin A1

Abstract Details of a technic for analysis of hemoglobin mixtures using acrylamide-gel electrophoresis are presented. The method offers increased speed and reproducibility. Measurements on the unstained gel are made at 525 and at 420 m µ in a procedure affording increased precision of measurements for minor components. The gel is then stained with amidoblack to detect and measure nonhemoglobin components. The major component of normal human adult hemoglobin is separated into two components in this medium. The two components (A1, A3) appear in varying relative amounts depending on the source of the specimen. The normal minor component A2 also appears. After staining the pattern with a protein dye such as amidoblack 10B, additional components appear in the electrophoresis patterns of hemolysates from carefully washed red cells. These components have a constant migration ratio referred to hemoglobin A1 and appear to be nonheme-containing intraerythrocytic proteins.

1H Nmr Studies of Cooperative Oxygenation of Normal Human Adult Hemoglobin

1982 ◽  
pp. 141-149 ◽  
Author(s):  
Chien Ho ◽  
Chi-Hon John Lam ◽  
Seizo Takahashi ◽  
Giulio Viggiano
Keyword(s):  
1H Nmr ◽  
Nmr Studies ◽  
Human Adult ◽  
Normal Human ◽  
Adult Hemoglobin

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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