[Validity of colposcopy-guided portio biopsy].
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Biomedical subjects
Publications and source records attributed to F Christensen.
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Elevated levels of alpha-1-fetoprotein (AFP) were found in the amniotic fluid of a 36-year-old woman in the 15th week of gestation. Because of this and the results of repeated ultrasonography, abortion was induced. An anencephalic fetus with trisomy 18 was delivered. The possible correlation among neural-tube defects, chromosomal abnormalities, and level of AFP is discussed.
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The inhibitory effect of chlorhexidine and other bis-biguanides on the formation of dental plaque is not fully understood. The present paper describes the effect of chlorhexidine and some selected detergents on the activity of dextransucrase (EC 2.4.1.5.), an enzyme involved in the formation of important components of dental plaque. All detergents examined exerted an inhibitory effect on dextransucrase activity, to some degree dependent on the presence of charged groups and their characters. The high concentrations of chlorhexidine necessary to inhibit dextransucrase activity seem to exclude the possibility that chlorhexidine exerts its plaque inhibiting effect by means of an effect on dextransucrase.
Human alpha1-antitrypsin was prepared from fresh human plasma by (NH4)-SO4-precipitation, gel filtration, affinity chromatography on concanavalin A, ion exchange chromatography and isotachophoresis. Human urokinase (EC 3.4.99.26) (plasminogen activator from urine) with M, 46 000 and 36 000 was further purified from Urokinase Leo reagent preparation by gel filtration on Sephadex G-100 Superfine. The hydrolytic activity of urokinase on acetyl-glycyl-L-lysine methyl ester acetate (Ac-Gly-Lys-OMeAc) was inhibited in a strong time-dependent manner by alpha1-antitrypsin. Complex formation between enzyme and inhibitor could be demonstrated in crossed immunoelectrophoresis against anti-alpha1-antitrypsin and anti-urokinase serum as well as by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The latter method revealed the formation of 1:1 and 2:1 molar enzyme-inhibitor complexes.
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