Prevention of hepatitis type B with specific immune serum globulin

In order to evaluate the preventive value of specific immune serum globulin against hepatitis type B, we have used this immune globulin in required doses in 12 patients (10 with AU antigen negative and 2 with AU antigen positive) with chronic renal failure who required maintenance hemodialysis for a period of 15 months, and we were able to prevent hepatitis type B in our dialysis patients.     

Pi (antitrypsin) typing methods. A comparison of acid starch-gel electrophoresis and isoelectric focusing

The Pi typing methods acid starch-gel electrophoresis (ASGE) and isoelectric focusing (IEF) have been compared by three reference laboratories: 564 samples of phenotypes Pi M, MS and MZ were tested in each of the three laboratories with a 96% agreement on initial typing. The discrepancies are recorded and reasons for disagreement discussed. IEF is a reliable method for Pi typing and gives results comparable to those obtained by ASGE.     

A spectrum of diseases of the thyroid gland as imaged by gray scale water bath sonography

A method of performing gray scale thyroid echography with a 3.5 MHz focused transducer and an open water bath is described. A preliminary echographic classification of abnormalities and representative echograms illustrating various thyroid disorders are presented.     

A G protein gamma subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gbeta5 subunits

Regulators of G protein signaling (RGS) proteins act as GTPase-activating proteins (GAPs) toward the alpha subunits of heterotrimeric, signal-transducing G proteins. RGS11 contains a G protein gamma subunit-like (GGL) domain between its Dishevelled/Egl-10/Pleckstrin and RGS domains. GGL domains are also found in RGS6, RGS7, RGS9, and the Caenorhabditis elegans protein EGL-10. Coexpression of RGS11 with different Gbeta subunits reveals specific interaction between RGS11 and Gbeta5. The expression of mRNA for RGS11 and Gbeta5 in human tissues overlaps. The Gbeta5/RGS11 heterodimer acts as a GAP on Galphao, apparently selectively. RGS proteins that contain GGL domains appear to act as GAPs for Galpha proteins and form complexes with specific Gbeta subunits, adding to the combinatorial complexity of G protein-mediated signaling pathways.