... Hún byggist á því að sérhæfðir griphópar eru notaðir til að veiða ákveðin lífefni úr blöndu e... more ... Hún byggist á því að sérhæfðir griphópar eru notaðir til að veiða ákveðin lífefni úr blöndu efna, svo sem útdráttarlausn úr lífveru sem inniheldur að jafnaði fjölmörg efni. ... Stoðefniðsvo rækilega þvegið og reynt að losna við alla óhvarfaða hópa sem ...
This is mainly a postoperative study of 33 male and female patients operated on for oesophageal h... more This is mainly a postoperative study of 33 male and female patients operated on for oesophageal hiatus hernia with the same technique, at the same hospital, by four different surgeons over a 5-year period. All the patients were followed up for a mean period of 2.8 years (range 11 months to 4 years 11 months). The patients were personally interviewed about the clinical (subjective) results of the operation and the outcome is compared with pre-operative symptoms. All underwent postoperative radiological examination with barium meal and the results are given. Further investigations on all available patients, who still had symptoms postoperatively, were carried out by oesophagogastroscopy, pH oesophageal reflux and acid perfusion tests. The result of these investigations are presented, evaluated and compared with clinical symptoms.
A low-molecular-weight biomimetic affinity ligand selective for binding elastase has been designe... more A low-molecular-weight biomimetic affinity ligand selective for binding elastase has been designed and synthesized. The ligand was based on mimicking part of the interaction between a natural inhibitor, turkey ovomucoid inhibitor and elastase, and modelled from the X-ray crystallographic structure of the enzyme-inhibitor complex. Limited solid-phase combinatorial chemistry was used to synthesize 12 variants of the lead ligand using the triazine moiety as the scaffold for assembly. The ligand library was screened for its ability to bind elastase and trypsin, and two ligands were studied further. Ligand C4/6 [2-alanyl-alanyl-4-tryptamino-6-(alpha-lysyl)-s-triazine] was found to bind porcine pancreatic elastase, but not trypsin, with a dissociation constant of 6 x 10(-5) M and a binding capacity of 21 mg elastase per ml gel. The adsorbent was used to purify elastase from a crude extract of porcine pancreas. Immobilized ligand C4/5 6 [2-alanyl-alanyl-4-tyramino-6-(alpha-lysyl)-s-triazine] was similarly chosen for optimal binding of elastase from cod and used to purify the enzyme from a crude extract of cod pyloric caeca. Ligand C4/6 was subsequently synthesized in solution and its structure verified by 1H-NMR.
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1998
Elastase was isolated from ovine pancreas and purified to homogeneity by two different procedures... more Elastase was isolated from ovine pancreas and purified to homogeneity by two different procedures. One involved precipitation with ammonium sulphate, p-aminobenzamidine-Sepharose chromatography, CM-Sepharose ion exchange chromatography and S-300 Sephacryl chromatography. The other involved the direct adsorption of elastase by tri-L-alanyl-Sepharose chromatography and a CM-Sepharose step. The enzyme, which was produced in an inactive form in the pancreas, was activated with a trace of trypsin prior to chromatography. Ovine pancreatic elastase has an isoelectric point above pI 9.3 and its molecular mass is estimated at approximately 25 kDa. The optimal pH range for activity is between 8.0 and 8.4 and the enzyme is unstable at pH below 4.0 and above 10.0 and at temperatures above 65 degrees C. The kinetic properties of the enzyme were determined with succinyl-Ala-Ala-Ala-p-nitroanilide as the substrate. Km and kcat Km-1 proved to be similar to the kinetic parameters of porcine elastase determined simultaneously.
Scandinavian journal of social medicine. Supplementum, 1984
In the first stage of a prospective cardiovascular health survey, 2955 males aged 34-61 years wer... more In the first stage of a prospective cardiovascular health survey, 2955 males aged 34-61 years were invited for examination during a 12-month period. The response was 75%. Appointments were arranged in such a way that all age groups would be equivalent with respect to time of day, weekday and time of year on which appointments were given. In fasting blood and urine samples the following quantities were estimated: s-alkaline phosphatase (AP), s-bilirubin (Bil), s-creatinine (Cre), s-uric acid (UA), haemoglobin (Hb), haematocrit (Hct), mean cell haemoglobin content (MCHC), erythrocyte sedimentation rate (ESR) and urine specific gravity (USG). The approximate 5% and 95% centiles were as follows: (table; see text) No indication of seasonal variation was found in these results.
1. A process is described for the chemical attachment of an enzyme to the surface of a polystyren... more 1. A process is described for the chemical attachment of an enzyme to the surface of a polystyrene matrix. 2. By this process yeast beta-fructofuranosidase was chemically attached to the surface of both polystyrene beads and polystyrene tubes. 3. The kinetics of sucrose hydrolysis by beta-fructofuranosidase and polystyrene-supported beta-fructofuranosidase were compared. 4. The pH-activity curve of the polystyrene-supported enzyme shows a marked difference from that of the free enzyme in solution. 5. The inhibitor dissociation constant with respect to tris is increased, whereas the inhibitor dissociation constant with respect to aniline is decreased when the enzyme is attached to polystyrene. 6. Differences between the properties of the bound and free enzyme are discussed in terms of a micro-environmental effect arising from the hydrophobic nature of the polystyrene support.
A low-molecular-weight biomimetic affinity ligand selective for binding elastase has been designe... more A low-molecular-weight biomimetic affinity ligand selective for binding elastase has been designed and synthesized. The ligand was based on mimicking part of the interaction between a natural inhibitor, turkey ovomucoid inhibitor and elastase, and modelled from the X-ray crystallographic structure of the enzyme-inhibitor complex. Limited solid-phase combinatorial chemistry was used to synthesize 12 variants of the lead ligand using the triazine moiety as the scaffold for assembly. The ligand library was screened for its ability to bind elastase and trypsin, and two ligands were studied further. Ligand C4/6 [2-alanyl-alanyl-4-tryptamino-6-(alpha-lysyl)-s-triazine] was found to bind porcine pancreatic elastase, but not trypsin, with a dissociation constant of 6 x 10(-5) M and a binding capacity of 21 mg elastase per ml gel. The adsorbent was used to purify elastase from a crude extract of porcine pancreas. Immobilized ligand C4/5 6 [2-alanyl-alanyl-4-tyramino-6-(alpha-lysyl)-s-triazine] was similarly chosen for optimal binding of elastase from cod and used to purify the enzyme from a crude extract of cod pyloric caeca. Ligand C4/6 was subsequently synthesized in solution and its structure verified by 1H-NMR.
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1996
Carboxylesterase ESB3 was extracted from ovine liver and purified to homogeneity by ammonium sulp... more Carboxylesterase ESB3 was extracted from ovine liver and purified to homogeneity by ammonium sulphate fractionation, hydrophobic interaction chromatography on Phenyl Sepharose, ion exchange chromatography on Mono-Q Sepharose and size exclusion chromatography on Superose 6. The enzyme is free of carboxylesterase ESB2 activity. The molecular mass of the enzyme is estimated 182 kDa as judged by size exclusion chromatography. Isoelectric focusing indicates the presence of six isoforms of pI 5.50-5.77 with three main isoforms of pI 5.55-5.65. The enzyme is active towards the substrates p-nitrophenyl acetate and the aliphatic substrates ethyl acetate, ethyl propionate, ethyl butyrate, and ethyl valerate. Of the ethyl esters the affinity is lowest towards acetate and highest towards ethyl butyrate. The enzyme is totally inhibited by phenylmethylsulphonyl fluoride (PMSF) and mercuric chloride but not affected by eserine or cupric chloride. The pH optimum of the enzyme is 7.5 and it is stable at 55°C for 20 min. coup BIOCHEM PHYSIOL l14B, 41-48, 1996.
... Hún byggist á því að sérhæfðir griphópar eru notaðir til að veiða ákveðin lífefni úr blöndu e... more ... Hún byggist á því að sérhæfðir griphópar eru notaðir til að veiða ákveðin lífefni úr blöndu efna, svo sem útdráttarlausn úr lífveru sem inniheldur að jafnaði fjölmörg efni. ... Stoðefniðsvo rækilega þvegið og reynt að losna við alla óhvarfaða hópa sem ...
This is mainly a postoperative study of 33 male and female patients operated on for oesophageal h... more This is mainly a postoperative study of 33 male and female patients operated on for oesophageal hiatus hernia with the same technique, at the same hospital, by four different surgeons over a 5-year period. All the patients were followed up for a mean period of 2.8 years (range 11 months to 4 years 11 months). The patients were personally interviewed about the clinical (subjective) results of the operation and the outcome is compared with pre-operative symptoms. All underwent postoperative radiological examination with barium meal and the results are given. Further investigations on all available patients, who still had symptoms postoperatively, were carried out by oesophagogastroscopy, pH oesophageal reflux and acid perfusion tests. The result of these investigations are presented, evaluated and compared with clinical symptoms.
A low-molecular-weight biomimetic affinity ligand selective for binding elastase has been designe... more A low-molecular-weight biomimetic affinity ligand selective for binding elastase has been designed and synthesized. The ligand was based on mimicking part of the interaction between a natural inhibitor, turkey ovomucoid inhibitor and elastase, and modelled from the X-ray crystallographic structure of the enzyme-inhibitor complex. Limited solid-phase combinatorial chemistry was used to synthesize 12 variants of the lead ligand using the triazine moiety as the scaffold for assembly. The ligand library was screened for its ability to bind elastase and trypsin, and two ligands were studied further. Ligand C4/6 [2-alanyl-alanyl-4-tryptamino-6-(alpha-lysyl)-s-triazine] was found to bind porcine pancreatic elastase, but not trypsin, with a dissociation constant of 6 x 10(-5) M and a binding capacity of 21 mg elastase per ml gel. The adsorbent was used to purify elastase from a crude extract of porcine pancreas. Immobilized ligand C4/5 6 [2-alanyl-alanyl-4-tyramino-6-(alpha-lysyl)-s-triazine] was similarly chosen for optimal binding of elastase from cod and used to purify the enzyme from a crude extract of cod pyloric caeca. Ligand C4/6 was subsequently synthesized in solution and its structure verified by 1H-NMR.
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1998
Elastase was isolated from ovine pancreas and purified to homogeneity by two different procedures... more Elastase was isolated from ovine pancreas and purified to homogeneity by two different procedures. One involved precipitation with ammonium sulphate, p-aminobenzamidine-Sepharose chromatography, CM-Sepharose ion exchange chromatography and S-300 Sephacryl chromatography. The other involved the direct adsorption of elastase by tri-L-alanyl-Sepharose chromatography and a CM-Sepharose step. The enzyme, which was produced in an inactive form in the pancreas, was activated with a trace of trypsin prior to chromatography. Ovine pancreatic elastase has an isoelectric point above pI 9.3 and its molecular mass is estimated at approximately 25 kDa. The optimal pH range for activity is between 8.0 and 8.4 and the enzyme is unstable at pH below 4.0 and above 10.0 and at temperatures above 65 degrees C. The kinetic properties of the enzyme were determined with succinyl-Ala-Ala-Ala-p-nitroanilide as the substrate. Km and kcat Km-1 proved to be similar to the kinetic parameters of porcine elastase determined simultaneously.
Scandinavian journal of social medicine. Supplementum, 1984
In the first stage of a prospective cardiovascular health survey, 2955 males aged 34-61 years wer... more In the first stage of a prospective cardiovascular health survey, 2955 males aged 34-61 years were invited for examination during a 12-month period. The response was 75%. Appointments were arranged in such a way that all age groups would be equivalent with respect to time of day, weekday and time of year on which appointments were given. In fasting blood and urine samples the following quantities were estimated: s-alkaline phosphatase (AP), s-bilirubin (Bil), s-creatinine (Cre), s-uric acid (UA), haemoglobin (Hb), haematocrit (Hct), mean cell haemoglobin content (MCHC), erythrocyte sedimentation rate (ESR) and urine specific gravity (USG). The approximate 5% and 95% centiles were as follows: (table; see text) No indication of seasonal variation was found in these results.
1. A process is described for the chemical attachment of an enzyme to the surface of a polystyren... more 1. A process is described for the chemical attachment of an enzyme to the surface of a polystyrene matrix. 2. By this process yeast beta-fructofuranosidase was chemically attached to the surface of both polystyrene beads and polystyrene tubes. 3. The kinetics of sucrose hydrolysis by beta-fructofuranosidase and polystyrene-supported beta-fructofuranosidase were compared. 4. The pH-activity curve of the polystyrene-supported enzyme shows a marked difference from that of the free enzyme in solution. 5. The inhibitor dissociation constant with respect to tris is increased, whereas the inhibitor dissociation constant with respect to aniline is decreased when the enzyme is attached to polystyrene. 6. Differences between the properties of the bound and free enzyme are discussed in terms of a micro-environmental effect arising from the hydrophobic nature of the polystyrene support.
A low-molecular-weight biomimetic affinity ligand selective for binding elastase has been designe... more A low-molecular-weight biomimetic affinity ligand selective for binding elastase has been designed and synthesized. The ligand was based on mimicking part of the interaction between a natural inhibitor, turkey ovomucoid inhibitor and elastase, and modelled from the X-ray crystallographic structure of the enzyme-inhibitor complex. Limited solid-phase combinatorial chemistry was used to synthesize 12 variants of the lead ligand using the triazine moiety as the scaffold for assembly. The ligand library was screened for its ability to bind elastase and trypsin, and two ligands were studied further. Ligand C4/6 [2-alanyl-alanyl-4-tryptamino-6-(alpha-lysyl)-s-triazine] was found to bind porcine pancreatic elastase, but not trypsin, with a dissociation constant of 6 x 10(-5) M and a binding capacity of 21 mg elastase per ml gel. The adsorbent was used to purify elastase from a crude extract of porcine pancreas. Immobilized ligand C4/5 6 [2-alanyl-alanyl-4-tyramino-6-(alpha-lysyl)-s-triazine] was similarly chosen for optimal binding of elastase from cod and used to purify the enzyme from a crude extract of cod pyloric caeca. Ligand C4/6 was subsequently synthesized in solution and its structure verified by 1H-NMR.
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1996
Carboxylesterase ESB3 was extracted from ovine liver and purified to homogeneity by ammonium sulp... more Carboxylesterase ESB3 was extracted from ovine liver and purified to homogeneity by ammonium sulphate fractionation, hydrophobic interaction chromatography on Phenyl Sepharose, ion exchange chromatography on Mono-Q Sepharose and size exclusion chromatography on Superose 6. The enzyme is free of carboxylesterase ESB2 activity. The molecular mass of the enzyme is estimated 182 kDa as judged by size exclusion chromatography. Isoelectric focusing indicates the presence of six isoforms of pI 5.50-5.77 with three main isoforms of pI 5.55-5.65. The enzyme is active towards the substrates p-nitrophenyl acetate and the aliphatic substrates ethyl acetate, ethyl propionate, ethyl butyrate, and ethyl valerate. Of the ethyl esters the affinity is lowest towards acetate and highest towards ethyl butyrate. The enzyme is totally inhibited by phenylmethylsulphonyl fluoride (PMSF) and mercuric chloride but not affected by eserine or cupric chloride. The pH optimum of the enzyme is 7.5 and it is stable at 55°C for 20 min. coup BIOCHEM PHYSIOL l14B, 41-48, 1996.
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