Bal-Therapy in Transfusion Hemosiderosis

Ohlsson, W. T. L.; Wilander, Olof

doi:10.1080/00365515409134828

Cited by 20 publications

(32 citation statements)

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“…The relative constancy of the specific inhibitor activity of (Xa-macroglobulin can be explained by the effective hepatic clearance of even low concentrations of <X2-macroglobülin-proteinase complexes from the circulation with a half-life in the order of 3 to 4 minutes (28,29), whereas that of a2-macroglobuliii itself is much longer (30). This mechanism prevents the accumulation of proteinase-burdened, i.e.…”

Section: Discussionmentioning

confidence: 99%

Amidolytic and Immuno-Nephelometric Determination of α1-Proteinase Inhibitor and α2-Macroglobulin in Serum with Calculation of Specific Inhibitor Activities in Health and Disease

Gressner¹,

Peltzer²

1984

Clinical Chemistry and Laboratory Medicine

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Summary:In sera of healthy persons (n = 50) and patients with a variety of diseases (n = 197) the two major proteinase inhibitors, αι-proteinase inhibitor (oti-antitrypsin) and ai-macroglobulin, were measured by two methods: a chromogenic (amidolytic) Substrate assay to assess the functional activities, and a laser nephelometric method to determine the immunoreactive concentrations of the respective proteins. The specific proteinase inhibitor activities defined s the number of inhibitor units per g inhibitor protein were calculated.The precision and accuracy of both assays were found to be similar, showing a satisfactory correlation of results for the sera of healthy persons (r ?= 0.916 for cta-macroglobulin and 0.988 for cti-proteinase inhibitor). In diseased individuals the correlation was lower than in normal persons (0.862 for a2-macroglobulin and 0.907 for αϊ-proteinase inhibitor). A poor correlation was obtained in patients with liver diseases (r = 0.586 for αι-proteinase inhibitor and 0.852 for ai-macroglobulin).Reference ranges were established for functional and immunological concentrations and for specific inhibitor activities, respectively. Normal values followed a Gaussian distribution.In patients with various diseases including those with acute phase response, the specific inhibitor activities of ctrproteinase inhibitor re reduced significantly; this is because inhibitor activity shows a smaller relative increase than immunoreactivity. Among the various diseases, no significant differences were noted. The specific inhibitor activity of az-macroglobulin changed significantly only in patients with carcinoma, liver diseases and trauma. Follow up of some patients shows also intraindividual Variation of specific proteinase inhibitor activities. Amidolytische und immun-nephelometrische Bestimmung von a/-Proteinase-Inhibitor und

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Section: Discussionmentioning

confidence: 99%

Amidolytic and Immuno-Nephelometric Determination of α1-Proteinase Inhibitor and α2-Macroglobulin in Serum with Calculation of Specific Inhibitor Activities in Health and Disease

Gressner¹,

Peltzer²

1984

Clinical Chemistry and Laboratory Medicine

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“…Bundy and Mehl [2] and Ohlsson [44] found that a,-antitrypsin was a more potent inhibitor of chymotrypsin than of trypsin. Although their experimental conditions were different from the present ones, these observations may conceivably explain their findings.…”

Section: Discussionmentioning

confidence: 99%

The Inhibition of Proteinases by Human α₁‐Antitrypsin

Hercz

1974

European Journal of Biochemistry

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The inhibition of human plasmin by a,-antitrypsin was time dependent and the rate of inhibition rapidly decreased with decreasing temperature.The effect of substrates on the inhibitions of trypsin and chymotrypsin was investigated. Theoretically the final degree of inhibition should be the same, whether the substrate is added to the proteinase-inhibitor system before or after the formation of the complex. The inhibition of chymotrypsin by a,-antitrypsin and of trypsin by commercial soybean trypsin inhibitor was in line with the prediction, with either casein or synthetic esters as substrates. However, in the trypsin-a,-antitrypsin system the degree of inhibition depended on the order in which the reactants were mixed. With both casein and p-tosyl-L-arginine methyl ester as substrates, inhibition was high when trypsin was preincubated with the inhibitor and the substrate was added later, and low or absent when the proteinase was added to the mixture of inhibitor and substrate.In the inhibition mixtures of plasmin, trypsin and chymotrypsin with a, -antitrypsin, distinct changes were detected by electrophoresis in polyacrylamide gel. The unreacted inhibitor diminished or disappeared and reaction products were formed at rates corresponding to rates of inhibition. a,-Antitrypsin, the most abundant proteinase inhibitor in human serum, exhibits a broad range of specificity toward proteinases. It is known to inhibit trypsin [I -41, chymotrypsin [2-41, elastase [3,5-81, plasmin [4,9-131, thrombin [4], collagenases [14,15] According to several authors the inhibition of trypsin and chymotrypsin by a,-antitrypsin is stoichiometric and is complete in a very short time [l -41. In contrast, the inhibition of kallikrein and plasmin is not strictly stoichiometric [4], is slow [3,4,10,11,16], and strongly temperature dependent [ 161. Acylation of a,-antitrypsin with maleic anhydride abolishes its trypsin-inhibiting capacity [ 19,201 suggesting that one or more lysine residues play a part in the binding process.Rimon et al. found that while inhibition of trypsin and chymotrypsin was not retarded in the presence of substrate, the inhbition of plasmin and thrombin was [4].I examined the reactions of plasmin, trypsin and chymotrypsin with a,-antitrypsin by inhibition studies. The effects of substrates on the inhibition of chymotrypsin were in good agreement with theoretical predictions, but on the inhibition of trypsin were not.The inhibition of the three different proteinases by a,-antitrypsin was accompanied by electrophoretically detectable changes, and the rate of these changes was about the same as the corresponding rate of inhibition.Some of these observations were included in a previous abstract [21].

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“…1 ) . 'The column (2.5 x 30 cm) was equilibrated with 0.05 M sodium acetate buffer, pH 6.0 containing 0.002 M calcium lactate. The column was eluted with a linear NaCl concentration gradient (400 ml or the acetate buffer without NaCl and 400 ml with 0.5 M NaCI).…”

Section: Purification Of Elastasementioning

confidence: 99%

“…The K, value for 3-carboxypropionyl-~-alanyl-~-alanyl-~-alanyl-~~-nitroanilide was 2.50 mM and the pH optimum 8. 5. The elastase preparation obtained was 99.57,) active as judged from active-site titration.…”

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confidence: 99%

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Isolation and Partial Characterization of Elastase from Dog Granulocytes

Delshammar¹,

Ohlsson²

1976

European Journal of Biochemistry

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An elastolytic enzyme has been isolated from dog granulocyte leukocytes. The purification procedure included preparation of the granula fraction, chromatography on Sephadex G‐75 and ion‐exchange chromatography on SP‐Sephadex C‐50 at pH 6.0. The elastase isolated was homogeneous in analytical disc electrophoresis and showed in sodium dodecylsulfate electrophoresis a single protein component with the molecular weight of 24800. The. enzyme lacked tyrosine and lysine and the N‐terminal amino acid was phenylalanine. No carbohydrate or sialic acid were detected. The dog granulocyte elastase showed similar activities as human granulocyte elastase on elastin and fibrin. The Km value for 3‐carboxypropionyl‐l‐alanyl‐l‐alanyl‐l‐alanyl‐p‐nitroanilide was 2.50 mM and the pH optimum 8.5. The elastase preparation obtained was 99.5%, active as judged from active‐site titration. The enzyme is a cationic protein and shows pronounced trailing on agarose gel electrophoresis. A monospecific antiserum against the purified enzyme was produced in rabbits.

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Bal-Therapy in Transfusion Hemosiderosis

Cited by 20 publications

References 0 publications

Amidolytic and Immuno-Nephelometric Determination of α1-Proteinase Inhibitor and α2-Macroglobulin in Serum with Calculation of Specific Inhibitor Activities in Health and Disease

Amidolytic and Immuno-Nephelometric Determination of α1-Proteinase Inhibitor and α2-Macroglobulin in Serum with Calculation of Specific Inhibitor Activities in Health and Disease

The Inhibition of Proteinases by Human α₁‐Antitrypsin

Isolation and Partial Characterization of Elastase from Dog Granulocytes

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Bal-Therapy in Transfusion Hemosiderosis

Cited by 20 publications

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Amidolytic and Immuno-Nephelometric Determination of α1-Proteinase Inhibitor and α2-Macroglobulin in Serum with Calculation of Specific Inhibitor Activities in Health and Disease

Amidolytic and Immuno-Nephelometric Determination of α1-Proteinase Inhibitor and α2-Macroglobulin in Serum with Calculation of Specific Inhibitor Activities in Health and Disease

The Inhibition of Proteinases by Human α1‐Antitrypsin

Isolation and Partial Characterization of Elastase from Dog Granulocytes

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The Inhibition of Proteinases by Human α₁‐Antitrypsin