The Experts below are selected from a list of 234 Experts worldwide ranked by ideXlab platform
Samuel O Sowemimocoker - One of the best experts on this subject based on the ideXlab platform.
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red blood cell Hemolysis during processing
Transfusion Medicine Reviews, 2002Co-Authors: Samuel O SowemimocokerAbstract:Red blood cell (RBC) Hemolysis has been reported in units of RBC for transfusion. This has significant clinical implications for transfused patients because the free hemoglobin dissociates into dimers that have to be bound to haptoglobin to be removed by the reticuloen-dothelial system. Once the binding capacity of haptoglobin has been exceeded, hemoglobinemia occurs. Hemolysis is caused by the breakdown of the RBC, causing release of hemoglobin and resulting in the discoloration of the plasma. Abnormal Hemolysis in an individual RBC unit may be caused by several factors including inappropriate handling during processing of blood, inappropriate storage conditions, bacterial hemolysins, antibodies that cause complement lysis, defects in the RBC membrane, or an abnormality in the blood donor. The degree of Hemolysis is described as the percent of free hemoglobin in relation to the total hemoglobin with appropriate correction for the hematocrit. The acceptable level of Hemolysis has not been established in North America, but the value of 1% currently is used to assess biocompatibility of blood storage materials, whereas the Council of Europe has set the standard at 0.8%. This report emphasizes the need for the adequate control of the various processes that are involved in the preparation of RBCs from whole blood to minimize the occurrence of Hemolysis. Careful evaluation of manufacturing processes will minimize RBC wastage caused by Hemolysis.
Denise V Tambourgi - One of the best experts on this subject based on the ideXlab platform.
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caissarolysin i bcs i a new hemolytic toxin from the brazilian sea anemone bunodosoma caissarum purification and biological characterization
Biochimica et Biophysica Acta, 2006Co-Authors: Joacir Stolarz De Oliveira, Andre Junqueira Zaharenko, Jose Carlos De Freitas, Katsuhiro Konno, Sonia A De Andrade, Fernanda C V Portaro, Michael K Richardson, O A Santanna, Denise V TambourgiAbstract:Abstract Two cationic proteins, C1 and C3, were purified to homogeneity from the hemolytic fraction of the venom of Bunodosoma caissarum sea anemone. The purification processes employed gel filtration followed by ion exchange chromatography, being the purity and molecular mass confirmed by SDS-PAGE and mass spectrometry. Protein C1 represented the second major peak of the hemolytic fraction and was previously believed to be a cytolysin belonging to a new class of hemolysins. The C1 protein has a molecular mass of 15495 Da and was assayed for Hemolysis, PLA2 activity and acute toxicity in crabs and mice, showing no activity in these assays. It has an amino terminal with no similarity to all known hemolysins and, therefore, should not be considered a toxin, being its function completely unknown. The protein C3 (19757 Da), that also lacks PLA2 activity, was recognized by antiserum against Eqt II and presented high hemolytic activity to human erythrocytes (ED50 of 0.270 μg/ml), being named Caissarolysin I (Bcs I). Its activity was inhibited by pre-incubation with sphingomyelin (SM) and also when in presence of erythrocytes pre-treated with the SMase P2, a phospholipase D from the brown spider Loxosceles intermedia, indicating that SM is the main target of Bcs I. Caissarolysin I is the first hemolysin purified from a sea anemone belonging to the genus Bunodosoma and belongs to the Actinoporin family of sea anemone hemolysins.
Andre Junqueira Zaharenko - One of the best experts on this subject based on the ideXlab platform.
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caissarolysin i bcs i a new hemolytic toxin from the brazilian sea anemone bunodosoma caissarum purification and biological characterization
Biochimica et Biophysica Acta, 2006Co-Authors: Joacir Stolarz De Oliveira, Andre Junqueira Zaharenko, Jose Carlos De Freitas, Katsuhiro Konno, Sonia A De Andrade, Fernanda C V Portaro, Michael K Richardson, O A Santanna, Denise V TambourgiAbstract:Abstract Two cationic proteins, C1 and C3, were purified to homogeneity from the hemolytic fraction of the venom of Bunodosoma caissarum sea anemone. The purification processes employed gel filtration followed by ion exchange chromatography, being the purity and molecular mass confirmed by SDS-PAGE and mass spectrometry. Protein C1 represented the second major peak of the hemolytic fraction and was previously believed to be a cytolysin belonging to a new class of hemolysins. The C1 protein has a molecular mass of 15495 Da and was assayed for Hemolysis, PLA2 activity and acute toxicity in crabs and mice, showing no activity in these assays. It has an amino terminal with no similarity to all known hemolysins and, therefore, should not be considered a toxin, being its function completely unknown. The protein C3 (19757 Da), that also lacks PLA2 activity, was recognized by antiserum against Eqt II and presented high hemolytic activity to human erythrocytes (ED50 of 0.270 μg/ml), being named Caissarolysin I (Bcs I). Its activity was inhibited by pre-incubation with sphingomyelin (SM) and also when in presence of erythrocytes pre-treated with the SMase P2, a phospholipase D from the brown spider Loxosceles intermedia, indicating that SM is the main target of Bcs I. Caissarolysin I is the first hemolysin purified from a sea anemone belonging to the genus Bunodosoma and belongs to the Actinoporin family of sea anemone hemolysins.
Pam Dandrea - One of the best experts on this subject based on the ideXlab platform.
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intradonor reproducibility and changes in hemolytic variables during red blood cell storage results of recall phase of the reds iii rbc omics study
Transfusion, 2019Co-Authors: Marion C Lanteri, Tamir Kanias, Mars Stone, Grier P Page, Donald Brambilla, Stacy M Endresdighe, Alan E Mast, Walter Bialkowski, Sheila M. Keating, Pam DandreaAbstract:BACKGROUND: Genetic determinants may underlie the susceptibility of red blood cells (RBCs) to hemolyze in vivo and during routine storage. This study characterized the reproducibility and dynamics of in vitro Hemolysis variables from a subset of the 13,403 blood donors enrolled in the RBC-Omics study. STUDY DESIGN AND METHODS: RBC-Omics donors with either low or high Hemolysis results on 4°C-stored leukoreduced (LR)-RBC samples from enrollment donations stored for 39 to 42 days were recalled 2 to 12 months later to donate LR-RBCs. Samples of stored LR-RBCs from the unit and from transfer bags were evaluated for spontaneous and stress-induced Hemolysis at selected storage time points. Intradonor reproducibility of Hemolysis variables was evaluated in transfer bags over two donations. Hemolysis data at serial storage time points were generated on LR-RBCs from parent bags and analyzed by site, sex, race/ethnicity, and donation frequency. RESULTS: A total of 664 donors were successfully recalled. Analysis of intradonor reproducibility revealed that osmotic and oxidative Hemolysis demonstrated good and moderate reproducibility (Pearson's r = 0.85 and r = 0.53, respectively), while spontaneous Hemolysis reproducibility was poor (r = 0.40). Longitudinal Hemolysis in parent bags showed large increases over time in spontaneous (508.6%) and oxidative Hemolysis (399.8%) and smaller increases in osmotic (9.4%) and mechanical fragility (3.4%; all p < 0.0001). CONCLUSION: Spontaneous Hemolysis is poorly reproducible in donors over time and may depend on site processing methods, while oxidative and osmotic Hemolysis were reproducible in donors and hence could reflect consistent heritable phenotypes attributable to genetic traits. Spontaneous and oxidative Hemolysis increased over time of storage, whereas osmotic and mechanical Hemolysis remained relatively stable.
Joacir Stolarz De Oliveira - One of the best experts on this subject based on the ideXlab platform.
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caissarolysin i bcs i a new hemolytic toxin from the brazilian sea anemone bunodosoma caissarum purification and biological characterization
Biochimica et Biophysica Acta, 2006Co-Authors: Joacir Stolarz De Oliveira, Andre Junqueira Zaharenko, Jose Carlos De Freitas, Katsuhiro Konno, Sonia A De Andrade, Fernanda C V Portaro, Michael K Richardson, O A Santanna, Denise V TambourgiAbstract:Abstract Two cationic proteins, C1 and C3, were purified to homogeneity from the hemolytic fraction of the venom of Bunodosoma caissarum sea anemone. The purification processes employed gel filtration followed by ion exchange chromatography, being the purity and molecular mass confirmed by SDS-PAGE and mass spectrometry. Protein C1 represented the second major peak of the hemolytic fraction and was previously believed to be a cytolysin belonging to a new class of hemolysins. The C1 protein has a molecular mass of 15495 Da and was assayed for Hemolysis, PLA2 activity and acute toxicity in crabs and mice, showing no activity in these assays. It has an amino terminal with no similarity to all known hemolysins and, therefore, should not be considered a toxin, being its function completely unknown. The protein C3 (19757 Da), that also lacks PLA2 activity, was recognized by antiserum against Eqt II and presented high hemolytic activity to human erythrocytes (ED50 of 0.270 μg/ml), being named Caissarolysin I (Bcs I). Its activity was inhibited by pre-incubation with sphingomyelin (SM) and also when in presence of erythrocytes pre-treated with the SMase P2, a phospholipase D from the brown spider Loxosceles intermedia, indicating that SM is the main target of Bcs I. Caissarolysin I is the first hemolysin purified from a sea anemone belonging to the genus Bunodosoma and belongs to the Actinoporin family of sea anemone hemolysins.
