Syk-C resembles other SH2 domains in its peptide-binding interactions and overall topology, a result that is consistent with its ability to function as an independent SH2 domain in vitro. This result suggests that Syk-C plays a unique role in the intact Syk protein. The determinants of the binding affinity and selectivity of Syk-C may reside in the least-conserved structural elements that comprise the phosphotyrosine- and leucine-binding sites. These structural features can be exploited for the design of Syk-selective SH2 antagonists for the treatment of allergic disorders and asthma.

A solid-phase sandwich radioimmunoassay was developed to quantitate human group-II pepsinogens in plasma. The test detected pepsinogen II in a concentration range of 0.25–64.0 ng/ml using sample volumes of 125 μl. Purified group I pepsinogens showed no response up to concentrations of 100 μg/ml. In apparently healthy donors, we observed mean plasma concentrations of 20.3 ng/ml (males) and of 15.5 ng/ml (females).

No abstract

No abstract

No abstract