Recent studies have demonstrated that bovine and primate aqueous humor (AH) obstruct flow when perfused through artificial membranes with pore sizes similar to those found in the aqueous outflow pathway. Proteinaceous AH components were implicated in this phenomenon, which is not observed with serum diluted to comparable protein concentrations. In this study, we used two-dimensional gel electrophoresis to characterize the protein composition of calf AH and to identify those proteins binding to the filters and presumably causing this obstruction. Comparison of AH and serum under denaturing conditions showed quantitative and qualitative differences in their protein content. Among the most important: AH was seen to possess two protein subunit trains (~28 kD and ~48 kD) not found in serum and two trains (~28 kD and ~80 kD) with additionally charged components not found in serum. Serum, on the other hand, possesses one train (~80-90 kD) not found in AH as well as a slightly greater relative amount of high-molecular weight protein subunits. The finding that hydrophobic filters retain more protein components than do hydrophilic filters suggests that the type and amount of protein adhering to them is determined largely by hydrophobic interactions. Whether such interactions occur in the outflow system, and if so, how they may relate to aqueous drainage remains to be determined.
|Number of pages
|Investigative Ophthalmology and Visual Science
|Published - 1989
ASJC Scopus subject areas
- Sensory Systems
- Cellular and Molecular Neuroscience