In 29 patients with community-acquired pneumonia, 24 patients with hospital-acquired pneumonia and 35 patients with pneumonia in the immunocompromised host the diagnostic value of bronchoalveolar lavage (BAL) with quantitative bacterial and fungal cultures was studied; 32 patients with noninfectious pulmonary diseases and 14 healthy volunteers served as controls. An infectious etiology could be established in 81% of the pneumonia patients without differences between the three groups; significant infection was associated with colony counts of > or = 10(4) cfu/ml. Prior antibiotic therapy lowered the yield of BAL culture only in community-acquired pneumonia (94% vs 55% positive cultures in untreated vs pretreated patients, p < 0.02). Furthermore the culture results were related to the radiographic extension of pulmonary infiltrates (92% positive cultures in multilobar vs 54% in lobar or segmental infiltrates, p < 0.001). Therapeutic consequences of BAL were shown by resistance of the isolated organisms to predefined empiric treatment regimens in 41% community-acquired pneumonia, 43% pneumonia in the immunocompromised host and 67% hospital-acquired pneumonia patients.
The isolation of an unspecific carboxylesterase from rat liver microsomes is reported. The purification is 66‐fold at a yield of about 20%. The enzyme is one of 5 esterase/amidase variants recently separated and corresponds to the fraction designated E1.
The enzyme is homogeneous in disc electrophoresis, dodecylsulfate‐polyacrylamide gel electrophoresis and in analytical ultracentrifugation, but exhibits slight heterogeneity in isoelectric focusing.
Its amino acid composition is presented.
The molecular weight of rat liver esterase E1 is 177000 (equilibrium sedimentation), the subunit weight 61 500 (dodecylsulfate disc electrophoresis), and the equivalent weight 66000 (titration with bis[p‐nitrophenyl]phosphate). After cross‐linking of the enzyme by dimethyl suberimidate and dodecylsulfate‐polyacrylamide gel electrophoresis three principal bands are observed. Therefore, a trimeric structure in which each subunit possesses one active site is proposed.
Properties of calf thymus chromatin, prepared by mild procedures, have been studied in various solvents. In 0.2 mM EDTA s-values ranged from 20 to 30 S and intrinsic viscosities from 5 to 24 dl/g. Dialysis against 0.15 M NaCl or 0.2 mM MgCl2 changed these values to 80 to 100 S and 0.2 to 5 dl/g, respectively, indicating an essentially more compact structure. In 0.2 mM EDTA X-ray scattering yielded a cross section diameter of 9 nm, which is associated with the tertiary structure of chromatin fiber (M/L = 21200 Dalton/nm). By dialysis against 0.15 M NaCl or 0.2 mM MgCl2 part of the material spontaneously formed quarterny structures (cross section diameters 25-29 nm). The rest of the material with cross section diameters less than 9 nm is supposed to be more strongly sheared tertiary structure which seems to be unable to form quarterny structure due to artificial conformational changes.
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