Divergent and common groups of proteins in glands of venomous snakes.

Protein contents of venom-producing glands from the sea-snake Laticauda colubrina (LC) and terrestrial Vipera Russelli (VR) were studied using high-resolution two-dimensional gels: isoelectric focusing followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (IEF/SDS-PAGE) and nonequilibrium pH gradient electrophoresis (NEPHGE) followed by SDS-PAGE. Tentative identities of numerous proteins were established using their amino acid compositions and in certain cases the identities were verified by microsequencing of their N-terminals and internal fragments. As expected, we found several proteins known to be present in the venom of the respective snakes.

The in vitro effect of lithocholic acid on the polymerization properties of PiZ alpha-1-antitrypsin.

We describe here an in vitro effect of lithocholic acid (LA), a secondary, hydrophobic bile acid, on the rate of polymerization of mutant, Z and wild-type, M alpha-1-antitrypsin (AAT). Using thioflavine T fluorescence and turbidity assays we demonstrated that the rate of aggregation for the Z AAT in the presence of LA at a molar ratio of 1:5 AAT to LA, in Tris-buffered saline, pH 7.4, is at least twice that of the Z protein alone or the M variant with and without LA.

Proteins and their amino acid compositions: uniqueness, variability, and applications.

Amino acid compositions (AAC) of proteins were analyzed in terms of their uniqueness and variability. Using several measures of convergence between the AACs of randomly chosen proteins versus those stored in protein data banks, it was established that certain families of proteins have unique AACs despite the mutations of their sequences which were imposed in the process of evolution. AACs may be used to establish the identities of many proteins which were sorted through various chromatographic media prior to their fractionation on two-dimensional (2D) gels.