Three-Dimensional Myocardial Perfusion Maps by Contrast Echocardiography.

We evaluated the clinical applicability of a system for three-dimensional (3-D) display of a perfusion map following myocardial contrast echocardiography (MCE). The system was used in 12 patients (9 males and 3 females, mean age 52 +/- 10 years) undergoing interventional treatment of chronic total coronary occlusion. In each patient three standard apical views were acquired at baseline with sonicated Iopamidol(R) injections into the left coronary artery (LCA) and into the right coronary artery (RCA).

[Limited proteolysis of human albumin and immunoglobulin G by Legionella pneumophila metalloproteinase].

Metalloproteinase of Legionella pneumophila is the major extracellular proteinase of this bacterial species which splits human immunoglobulin G in the hinge region to form the (Fab')2 fragment. This fragment is relatively stable and undergoes further proteolysis at a slow rate. The c' fragment is unstable and is apparently split down to fragments CH2 and CH3.

[The effect of Legionella pneumophila metalloproteinase on certain human blood proteins. Cleavage of anti(1)-antitrypsin and acid-stable serine proteinase inhibitors].

Antitryptic activity of human blood serum was decreased after incubation with metalloproteinase from Legionella pneumophila. The enzymatic activity depends on the time of incubation as well as on the ratio between the enzyme content and blood serum total protein. Cross immunoelectrophoresis, involving monospecific rabbit antiserum towards the alpha 1-antitrypsin, demonstrated highly effective hydrolysis of alpha 1-antitrypsin by the metalloproteinase.

[Amino acid sequence in the reactive site region of an acid-stable inhibitor of trypsin, chymotrypsin and intracellular proteinases from rabbit serum].

The thermo- and acid-stable trypsin, chymotrypsin and intracellular proteinases inhibitor (TAS-inhibitor) from rabbit serum was digested by trypsin, and its domain (Mr 6200) with antitryptic activity was obtained in homogeneous state. The N-terminal amino acid sequence of this domain was established by automatic Edman degradation: Thr-Val-Ala-Ala-Cys-Asx-Leu-Pro-Ile-Val-Pro-Gly-Pro-X-Arg-Gly-Ile-Phe-X- Leu-X-Ala-Phe-X-Ala-Val-X-Gly. A high degree of homology of the primary structures rabbit, human and bovine TAS-inhibitors was demonstrated.