Zobrazeno 1 - 10
of 162
pro vyhledávání: '"N Shaklai"'
Autor:
N Shaklai, H R Ranney
The binding of hemoglobin to phosphatidylserine liposomes was studied by Hb quenching of the fluorescence intensity of 12-(9-anthroyl) stearic acid embedded in the lipid membrane. The interaction is basically electrostatic. Hb A2 interacts more stron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b91d59de2a23dc9c7d4ac79a78552e2b
https://doi.org/10.1159/000403121
https://doi.org/10.1159/000403121
Publikováno v:
International journal of laboratory hematology. 33(6)
Haemoglobin (Hb) quantification in whole blood is possible by various spectrophotometric methods. However, determination of low-level Hb in erythroid precursors or haemolytic plasma is inaccurate because of contribution from light scatter and/or nonh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::73c7a24af99cf6934b9b15cf096a36de
https://pubmed.ncbi.nlm.nih.gov/21631892
https://pubmed.ncbi.nlm.nih.gov/21631892
Publikováno v:
In Vitro Cellular & Developmental Biology - Animal. 29:636-642
Effects of free hemin on myocardium were investigated using a model of neonatal myocyte primary cultures. Cells were subjected to free hemin at concentrations up to 20 microM and equilibrated for 5 h at 37 degrees C. Distribution of hemin in media, c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d81c7e592b011d951016d4b5cc4d801
https://doi.org/10.1007/bf02634552
https://doi.org/10.1007/bf02634552
Publikováno v:
Advances in experimental medicine and biology. 454
Myoglobin (Mb), the muscular oxygen reservoir, was shown to possess peroxidative reactivity in presence of H2O2 leading to oxidation of isolated cellular proteins like myosin. The objective of this study was to investigate the peroxidative effect of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cad8938c668708e1abdc85bdeac499a3
https://pubmed.ncbi.nlm.nih.gov/9889895
https://pubmed.ncbi.nlm.nih.gov/9889895
Autor:
Y I, Miller, N, Shaklai
Publikováno v:
Biochemistry and molecular biology international. 34(6)
This study investigated free hemin induced modifications in low density lipoprotein (LDL). By use of fluorescent probes hemin was found to associate with LDL thereby inducing peroxidation of both lipids and protein. Upon LDL peroxidation, covalent cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6135e9c5deb80499efe8d5c941705642
https://pubmed.ncbi.nlm.nih.gov/7696984
https://pubmed.ncbi.nlm.nih.gov/7696984
Publikováno v:
Biochemistry international. 26(1)
The effect of myoglobin, free hemin and H2O2 on myosins from heart and skeletal muscle was studied. SDS-gel electrophoresis revealed that each agent caused intermolecular thiol crosslinking of both myosins dissociable by excess of beta-mercaptoethano
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8806ce55d7be63339bb98a54b26b92c5
https://pubmed.ncbi.nlm.nih.gov/1616493
https://pubmed.ncbi.nlm.nih.gov/1616493
Publikováno v:
Proceedings of the National Academy of Sciences. 78:65-68
The interactions of hemoglobin S with the erythrocyte membrane were compared with the corresponding interactions of hemoglobin A by measuring in both steady-state and kinetic experiments the quenching of the fluorescence of a probe embedded in erythr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::302d58bb1bddef277bf0f7d19ab47862
https://doi.org/10.1073/pnas.78.1.65
https://doi.org/10.1073/pnas.78.1.65
Publikováno v:
Journal of Biological Chemistry. 259:3812-3817
Approximately 10% of the albumin in normal human serum is modified by nonenzymatic glycosylation, primarily at the epsilon-amino group of lysine residue 525. Incubation of albumin with glucose under physiological conditions in vitro resulted in glyco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e357d43b1daee1740ce231dbf661341
https://doi.org/10.1016/s0021-9258(17)43168-1
https://doi.org/10.1016/s0021-9258(17)43168-1
Publikováno v:
Journal of Biological Chemistry. 256:1544-1548
The equilibria and kinetics of the reaction of heme-hemopexin with CO were studied. A stoichiometry of one CO/heme was determined, and the affinity of heme-hemopexin for CO was found to be pH-dependent. At pH 8.0, the affinity constant was 4.5 X 10(5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1bcb0975c06abeea0f6d1cad11cb92f4
https://doi.org/10.1016/s0021-9258(19)69838-8
https://doi.org/10.1016/s0021-9258(19)69838-8
Autor:
N. Dadosh, N. Shaklai
Publikováno v:
Photochemistry and Photobiology. 47:689-697
— Membrane cytoskeletons were separated by use of TritonX–100 from freshly isolated red cells, fixed with glutaraldehyde and their morphology was followed by scanning electron microscopy. At 37°C and pH 6.5 cytoskeletons retained cell-like shape
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab404cdad21a39d7d9ccd912b1031c10
https://doi.org/10.1111/j.1751-1097.1988.tb02766.x
https://doi.org/10.1111/j.1751-1097.1988.tb02766.x