{"title":"Resonance Raman spectroscopy of chemically modified hemoglobins.","authors":"F J Bruzzese, J A Dix, R P Rava, L C Cerny","doi":"10.3109/10731199009117297","DOIUrl":"https://doi.org/10.3109/10731199009117297","url":null,"abstract":"<p><p>Hemoglobin obtained from out-dated human blood was stripped of 2,3-diphosphoglycerate and modified with the crosslinking agents glyoxalic acid, 1,2-cyclohexadione, or fumarate to stabilize the tetramer. The resulting hemoglobins, which show alterations in their oxygen transport capability, have been studied in their oxy, deoxy and fluoro-met forms using resonance Raman spectroscopy with Soret excitation. The resonance Raman spectra of oxy-hemoglobins cross linked with glyoxalic acid and 1,2-cyclohexadione show that these cross linking agents force the heme into a high spin structure. The resonance Raman spectra of the fluoro-met hemoglobins, however, indicate that the same cross linking agents force the heme into a lower spin structure. Absorption spectroscopy and molecular orbital considerations suggest that protein constraints at the sixth ligand of the heme can account for the change in spin state in the glyoxalic acid and 1,2-cyclohexadione cross linked hemoglobins.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 2","pages":"143-56"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117297","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13518751","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
C D Smith, S T Schuschereba, J R Hess, L A McKinney, D Bunch, P D Bowman
{"title":"Liver and kidney injury after administration of hemoglobin cross-linked with bis(3,5-dibromosalicyl) fumarate.","authors":"C D Smith, S T Schuschereba, J R Hess, L A McKinney, D Bunch, P D Bowman","doi":"10.3109/10731199009117305","DOIUrl":"https://doi.org/10.3109/10731199009117305","url":null,"abstract":"<p><p>Human hemoglobin cross-linked between the alpha chains with bis (3,5-dibromosalicyl) fumarate (DBBF-Hb) was exchange transfused in swine and the histomorphologic changes were evaluated. Following exchange, animals were euthanized and tissues were taken for light and electron microscopy at 7.5 hours and days 1, 4, 7, and 15. Consistent hepatocellular and renal epithelial cell changes were seen. Hepatic injury, evident at 7.5 hours as cellular vacuolization, progressed to necrosis and acute inflammatory cell infiltration by days 1 and 4, was resolving by 7 days and was completely resolved by day 15. Cytochemical stains for iron and hemoglobin revealed positive material in Kupffer cells, endothelial cells, and necrotic hepatocytes. Rabbit anti-human hemoglobin antibody staining revealed immunoreactive material diffusely present at days 1 and 4 and limited to solitary hepatocytes by day 15. Kidney injury began as proximal tubular epithelial vacuolization and intraluminal casts progressing to tubular necrosis by 24 hours, with resolution by day 15. Iron and hemoglobin stains demonstrated these materials in the early lesions. Immunocytochemistries demonstrated human hemoglobin that remained as late as day 15. Electron microscopy revealed degeneration and regeneration of epithelial cells. The renal lesions were consistent with hemoglobinuria. The liver lesion was less well defined but was self limited.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 2","pages":"251-61"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117305","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13518758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A screening test for modified hemoglobin blood substitutes before clinical use: based on C3a complement activation in human plasma.","authors":"T M Chang, C Lister","doi":"10.3109/10731199009117339","DOIUrl":"https://doi.org/10.3109/10731199009117339","url":null,"abstract":"<p><p>Modified hemoglobin preparations may potentially cause hypersensitivity and anaphylactic reactions, antibody-antigen reactions and other problems. Unfortunately response in animal safety studies may not reflect the same response in human. The next best test before clinical trial in human may the use of human plasma in-vitro. This paper present an in-vitro procedure based on complement activation (C3a) of human plasma. The procedure involves collecting heparinised blood and separating the plasma and freezing the heparinised plasma at -70 degrees C until use. Each 100 lambda of control or test samples is added to 400 lambda of this plasma. This is incubated at 37 degrees C, 60 rpm for 1 hour, then added to EDTA saline to stop the reaction and stored at -70 degrees C until analysed by standard radioimmunoassay for C3a. (C3 measurement is not sensitivity enough). Using the screening test procedure described above, C3a levels (ng/ml) in plasma were: control, 1,980 +/- 280; Zymosan, 20,000; Hemoglobin preparation A, 2,227 +/- 617; Hemoglobin preparation B, 4,967 +/- 153; A 75% + B 25%, 3,967 +/- 270; A 50% + B 50%, 4,553 +/- 517; A 25% + B 75%, 4,920 +/- 430. Hemoglobin preparation A did not cause significant increases in C3a complement activation. Hemoglobin preparation B caused significant increase in C3a complement activation. Serial dilution of Hemoglobin preparation B in Hemoglobin preparation A continued to cause the same degree of C3a complement activation. This is not due to C3 exhaustion because Zymosan resulted in C3a of greater than 20,000ng/ml. This appears to show that this screening test can detect complement activation even at low concentrations of the hemoglobin preparation.(ABSTRACT TRUNCATED AT 250 WORDS)</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 5","pages":"693-701"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117339","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13253906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Characteristics of immobilized aminoacylase from Aspergillus oryzae on macroporous copolymers.","authors":"B L He, P Jiang, Y B Qiu","doi":"10.3109/10731199009117315","DOIUrl":"https://doi.org/10.3109/10731199009117315","url":null,"abstract":"<p><p>Aminoacylase from Aspergillus oryzae was adsorbed on functionallized macroporous copolymers where the enzyme showed excellent catalyzing activity and operation stability. Various factors which effect the activity of the immobilized aminoacylase such as temperature, pH and ionic strength were investigated. The continuous operation of the enzyme immobilized on macroporous copolymers was compared with that of the enzyme immobilized on DEAE-Sephadex.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 3","pages":"375-82"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117315","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13533365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The influence of vaccines and hyper immune serums on protein/platelet interaction towards an artificial surface.","authors":"T Chandy, C P Sharma","doi":"10.3109/10731199009117317","DOIUrl":"https://doi.org/10.3109/10731199009117317","url":null,"abstract":"<p><p>Protein adsorption and platelet adhesion are two important biological processes arising at the blood prosthetic interface. The effect of certain commonly used vaccines and hyper immune serums namely tetanus toxoid, tetanus immunoglobulin, polyvalent anti-snake venum serum and anticholera vaccine to modulate the surface induced platelet adhesion to polycarbonate substrate was investigated using washed calf platelets in presence and absence of fibrinogen. This study also demonstrated the changes in protein-surface binding with few of these vaccines, using SDS - polyacrylamide gel electrophoresis. It seems, the addition of tetanus toxoid to the polymer-protein system increased the level of surface-bound albumin and reduced the fibrinogen-surface attachment. On the other hand, tetanus immunoglobulin reversed the effect. This itself may be one of the parameters for the observed reduction in platelet-surface attachment due to tetanus toxoid. The enhanced platelet adhesion with other vaccines, may be correlated with the availability of more fibrinogen receptors for the platelets to attach. A better understanding of the mechanism of these vaccines is needed in vivo conditions for interrelating these findings.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 3","pages":"403-21"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117317","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13533367","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Co-immobilization and interaction of heparin and plasmin on collageno-elastic tubes.","authors":"H Shankar, F Senatore, D R Wu, S Avantsa","doi":"10.3109/10731199009117289","DOIUrl":"https://doi.org/10.3109/10731199009117289","url":null,"abstract":"<p><p>Heparin and plasmin were co-immobilized on collageno-elastic tubes (CETs) in order to develop a thromboresistant and fibrinolytic vascular prosthesis. The mutual interaction between heparin and plasmin both in the soluble and in the immobilized state was studied. The immobilization condition rendering maximum co-immobilized heparin and plasmin activity was identified to require heparin immobilization followed by plasmin immobilization. Soluble heparin exerts a positive synergistic effect on soluble plasmin. Immobilized heparin enhances plasmin loading on the CET as compared to the heparin-free graft. Heparin, in both the soluble or immobilized state, significantly decreases the Michaelis-Menten (M-M) parameter Km for immobilized plasmin over heparin-free immobilized plasmin. Furthermore, the M-M parameter Vmax for the immobilized plasmin in the presence of heparin decreases over heparin-free immobilized plasmin. These results suggest a decrease in the kinetic constant k3 for heparin-modified immobilized plasmin over the heparin-free form. Co-immobilized heparin-plasmin collagenous grafts represent a unique advance in the development of fibrinolytically active prostheses.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 1","pages":"59-73"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117289","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13294351","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
R Marangoni, F Civardi, F Masi, C Avanzi, R Savino, A Manfredi, R Cimino
{"title":"Improvement of continuous arteriovenous hemofiltration (CAVH) and hemofiltration (HF) efficiency by adding hemoperfusion (HP).","authors":"R Marangoni, F Civardi, F Masi, C Avanzi, R Savino, A Manfredi, R Cimino","doi":"10.3109/10731199009119631","DOIUrl":"https://doi.org/10.3109/10731199009119631","url":null,"abstract":"<p><p>Aiming to improve the efficiency of the blood purification convective methods either with spontaneous (CAVH) or with pump-assisted (HF) extracorporeal circulation we inserted after the hemofilter a cartridge containing 70 g of collodion-coated activated charcoal (CAC) microencapsulated, obtaining so hemofiltration and hemoperfusion in series (HF+HP). The obtained results show that in both methods HP addition gives a negligible increase of urea clearance and a practically null increase of phosphate clearance, whereas creatinine and uric acid clearances increase is remarkable especially, in percentage, with low blood flows (CAVH). In the HF+HP system we have also been studying B2-microglobulin (B2-M) clearance aiming at examining the possibility of increasing the removal of substances with higher molecular weight. We have been finding HP addition increases further on B2-M clearance already high in HF. Therefore we think HP addition to convective methods is an interesting step in the attempt to carry out highly efficient blood purification methods.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 4","pages":"541-8"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009119631","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13437114","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Stable perfluorocarbon emulsions using XMO-10 as surfactant: potential oxygen-carrying plasma expanders.","authors":"N Jing, B A Cooper","doi":"10.3109/10731199009117292","DOIUrl":"https://doi.org/10.3109/10731199009117292","url":null,"abstract":"<p><p>XMO-10, a perfluorocarbon surfactant produced emulsions of a perfluorocarbon (Perfluorotripropylamine, FTPA) in vitro which were stable at a range of temperatures for at least 5 days. Most of the emulsion particles were smaller than 1 micron, and all emulsion particles were of these dimensions when the emulsification mixture included 2% lecithin. XMO-10 produced more stable emulsions with smaller particles than did PF68, a widely-used emulsifying agent. XMO-10 was toxic to cells in culture but this toxicity was reduced or abolished when the XMO-10 was emulsified with perfluorocarbon. XMO-10 and lecithin produced relatively stable emulsions of perflurodecalin. Such emulsions, if non-toxic in vivo, might permit excretion of perfluorocarbon through the lungs and thus would permit infusion of sufficient quantities of the preparations to function in oxygen transport in severely anemic animals and man.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 1","pages":"107-17"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117292","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13486121","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
H Gin, B Dupuy, D Bonnemaison-Bourignon, L Bordenave, R Bareille, M J Latapie, C Baquey, J H Bezian, D Ducassou
{"title":"Biocompatibility of polyacrylamide microcapsules implanted in peritoneal cavity or spleen of the rat. Effect on various inflammatory reactions in vitro.","authors":"H Gin, B Dupuy, D Bonnemaison-Bourignon, L Bordenave, R Bareille, M J Latapie, C Baquey, J H Bezian, D Ducassou","doi":"10.3109/10731199009117287","DOIUrl":"https://doi.org/10.3109/10731199009117287","url":null,"abstract":"<p><p>The biocompatibility of polyacrylamide microcapsules was investigated by implanting microcapsules in the peritoneal cavity or the spleen of rats. The capsules were retrieved every four weeks for twenty weeks. They remained isolated and free in the peritoneal cavity, but led to a slight inflammatory reaction in the spleen. These results were confirmed, in vitro, by determinations of chemiluminescence and interleukin I levels, and by evaluation of attachment and growth of human fibroblasts. The microcapsules did not enhance these inflammatory reactions, and they were a poor support for cellular proliferation.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 1","pages":"25-42"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117287","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13486123","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Usual physicochemical criteria provide insufficient evidence that a functional hemoglobin solution can be used for transfusions after storage for 36 months at +4 degrees C.","authors":"P Menu, P Labrude, C Vigneron","doi":"10.3109/10731199009117299","DOIUrl":"https://doi.org/10.3109/10731199009117299","url":null,"abstract":"<p><p>Hemoglobin solutions will be of clinical interest only if they are easy to use, efficient and can be stored for long periods. While most studies are concerned with hemoprotein improvement (P50 and plasmatic half-life) few deal with long term stability of liquid state solutions. Physicochemical and physiological analyses were carried out on a 70 g/l ready-to-use hemoglobin solution after 1.5, 2.5 and 3 years storage at +4 degrees C, away from light and without any protective additives. The evaluation of hemoglobin stability by tests used in clinical biology shows few structural and functional alterations. However, after 1.5 year total transfusional exchanges carried out on rats cause rapid death, which seems to point to hemoprotein modifications undetected by biological techniques. It therefore appears that physicochemical tests do not provide adequate grounds for claiming that a hemoglobin solution kept for over a year and a half at +4 degrees C can still be used effectively in transfusions.</p>","PeriodicalId":77498,"journal":{"name":"Biomaterials, artificial cells, and artificial organs","volume":"18 2","pages":"169-81"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199009117299","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13518753","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}