scholarly journals The initial noncovalent binding of glucose to human hemoglobin in nonenzymatic glycation

Glycobiology ◽  
2013 ◽  
Vol 23 (11) ◽  
pp. 1250-1259 ◽  
Author(s):  
S. L. Clark ◽  
A. E. Santin ◽  
P. A. Bryant ◽  
R. Holman ◽  
K. J. Rodnick
Keyword(s):  
Human Hemoglobin ◽  
Nonenzymatic Glycation ◽  
Noncovalent Binding

scholarly journals Potential roles of inorganic phosphate on the progression of initially bound glucopyranose toward the nonenzymatic glycation of human hemoglobin: Mechanistic diversity and impacts on site selectivity

2018 ◽  
Vol 4 (1) ◽  
pp. 1425196 ◽  
Author(s):  
Brandy A. Smith ◽  
Christina R. Mottishaw ◽  
Andria J. Hendricks ◽  
Jason Mitchell ◽  
Stephanie Becker ◽  
...  
Keyword(s):  
Inorganic Phosphate ◽  
Human Hemoglobin ◽  
Nonenzymatic Glycation ◽  
Site Selectivity

Environmentally Friendly Preparation of Magnetic Composites Featuring Proteolytic Properties

INEOS OPEN ◽  
2020 ◽  
Author(s):  
N. A. Samoilova ◽  
Keyword(s):  
Enzyme Immobilization ◽  
Maleic Acid ◽  
Environmentally Friendly ◽  
Synthetic Polymer ◽  
Magnetic Composites ◽  
Interpolyelectrolyte Complex ◽  
Hydrolysis Rates ◽  
Poly Ethylene ◽  
Noncovalent Binding

The enzyme-containing magnetic composites are presented. The magnetic matrix for enzyme immobilization is obtained by sequential application of an amine-containing polysaccharide—chitosan and a synthetic polymer—poly(ethylene-alt-maleic acid) to the magnetite microparticles to form the interpolyelectrolyte complex shell. Then, the enzyme (trypsin) is immobilized by covalent or noncovalent binding. Thus, the suggested composites can be readily obtained in the environmentally friendly manner. The enzyme capacity of the resulting composites reaches 28.0–32.6 mg/g. The maximum hydrolysis rates of the H-Val-Leu-Lys-pNA substrate provided by these composites range within 0.60·10–7–0.77·10–7 M/min.

Interaction of human hemoglobin with oxygen in the presence of benzene and use of computer for construction of saturation curves

1986 ◽  
Vol 51 (8) ◽  
pp. 1795-1801
Author(s):  
Hana Hájková ◽  
Zdeněk Pavlíček ◽  
Vítěz Kalous
Keyword(s):  
Oxygen Saturation ◽  
Oxygen Pressure ◽  
Time Profile ◽  
Partial Oxygen Pressure ◽  
Human Hemoglobin ◽  
Allosteric Interaction ◽  
Partial Oxygen

The time profile of changes in the oxygen saturation curves of human hemoglobin in the presence of benzene was investigated. The partial oxygen pressure p50, necessary for a half saturation, decreases during the first 3.5 h of interaction of hemoglobin with benzene and did not change afterwards. The character of changes in Hill's coefficient was similar. The oxygen saturation was modeled both for hemoglobin alone and, using MWC as a model of allosteric interaction, also for hemoglobin and benzene in a computer.

scholarly journals The Kinetics of Ligand Binding and of the Association-Dissociation Reactions of Human Hemoglobin

1971 ◽  
Vol 246 (9) ◽  
pp. 2796-2807 ◽  
Author(s):  
Melvin E. Andersen ◽  
J. Keith Moffat ◽  
Quentin H. Gibson
Keyword(s):  
Ligand Binding ◽  
Human Hemoglobin ◽  
Kinetics Of

scholarly journals Structural effects in alkyl nitrite oxidation of human hemoglobin.

1984 ◽  
Vol 259 (1) ◽  
pp. 80-87
Author(s):  
M P Doyle ◽  
R A Pickering ◽  
J da Conceição
Keyword(s):  
Human Hemoglobin ◽  
Structural Effects ◽  
Nitrite Oxidation ◽  
Alkyl Nitrite

scholarly journals The Structure of Human Hemoglobin

1963 ◽  
Vol 238 (6) ◽  
pp. 2016-2027 ◽  
Author(s):  
Jack Goldstein ◽  
William Konigsberg ◽  
Robert J. Hill
Keyword(s):  
Human Hemoglobin

scholarly journals The Interactions between α and β Chains of Human Hemoglobin

1968 ◽  
Vol 243 (8) ◽  
pp. 1971-1978 ◽  
Author(s):  
E J Neer ◽  
W Konigsberg ◽  
G Guidotti
Keyword(s):  
Human Hemoglobin

scholarly journals Covalent alteration of the prosthetic heme of human hemoglobin by BrCCl3. Cross-linking of heme to cysteine residue 93.

1992 ◽  
Vol 267 (13) ◽  
pp. 8739-8743
Author(s):  
J.T. Kindt ◽  
A Woods ◽  
B.M. Martin ◽  
R.J. Cotter ◽  
Y Osawa
Keyword(s):  
Cysteine Residue ◽  
Cross Linking ◽  
Human Hemoglobin
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