Research and Scholarship Repository
The Research and Scholarship Institutional Repository collects, preserves, and showcases the scholarly achievements of Texas State University's academic community. It provides open access to the diverse array of research and scholarship materials created at Texas State including articles, presentations, posters, electronic theses and dissertations, capstones, multimedia presentations, and more.
More information: https://guides.library.txstate.edu/institutional-repository
Communities in DSpace
Select a community to browse its collections.
- Research centers and institutes supporting scholarly and creative activities across the university.
- Research, creative, and scholarly works created by the university community organized by college.
- Texas State University divisions, offices, and other interdisciplinary teams across campuses.
- Academic publications and conference proceedings from members of the university community.
- Electronic theses and dissertations, and graduate and undergraduate Capstones and Directed Research.
Recent Submissions
Shakespeare and Fletcher's Chaucerian Greeks: The Knight's Tale and The Two Noble Kinsmen
(1988-06) Bonds, Lawrence I.; Laird, Edgar S.; Skerpan, Elizabeth; Wright, Loyd S.
No abstract prepared.
Effects of Temperature on Egg Production and Early Life Stages of Fountain Darters
(1996-05) Bonner, Timothy H.; Whiteside, Bobby G.; Brandt, Thomas M.; Huffman, David G.
Studies were conducted to determine the effects of water temperature on egg and larvae production, larvae survival, and juvenile growth of the endangered fountain darter Etheostoma fonticola. Adult fish were exposed to water temperatures of 14, 17, 20, 23(control), 25, 27, and 29°C for 33 d. Egg production was significantly higher for fish held at 14, 17, 20, 23, and 25°C than fish held at 27 and 29°C. Percent hatch was significantly higher at temperatures of 14, 17, 20, and 23°C than at temperatures of 25, 27, and 29°C. Larval production was significantly higher at temperatures of 17, 20, and 23°C than temperatures of 14, 25, 27, and 29°C. Lethal temperatures for 50% mortalities of 24-to 72-h old larvae were estimated at 3.8 and 3 l.9°C over a 24-h period. Low survival and inconsistent growth data prevented an assessment of temperature effects on juvenile growth.
The Young England Party: An Analysis of Disraeli's Solution for English Social and Political Ills
(1965-05) Bolieu, Louis S.; Hudson, Gertrude; Young, Ione; Hayes, Barry
No abstract prepared.
Dialysis Studies on the Hydrolytic Products of Bovine Serum Albumin, II
(1962-08) Bohac, Rudy J.; Willms, Charles R.; Parks, Archie O.; Gregg, Cecil M.
No abstract prepared.
Analysis of an [Alpha]-Actinin-Like Protein That May Cross-Link Intermediate Filaments and Microfilaments
(1997-05) Bolanos, Sandra H.; Koke, Joseph R.; Garcia, Dana M.; Irvin, James D.
We previously described a novel intermediate filament-associated protein (IFAP) designated the G.3.5 antigen (after the monoclonal antibody that recognizes it). This IFAP has been found in a variety of tissue types including human and rat astrocytes (Malhotra et al., 1984b), rat skeletal and cardiac myocytes (Price et al., 1993), fibroblasts (Malhotra et al,, 1984a), rat hepatocytes (Jeffcoat et al., 1995), and chicken (Garcia, personal communication) and fish retinal tissues (Zamora et al., 1994). The G.3.5 antigen has been purified from rat skeletal and cardiac muscle (Price et al., 1993) and from bovine skeletal muscle (Jeffcoat et al., 1995). The G.3.5 antigen is an IFAP that colocalizes with desmin in skeletal and cardiac myocytes. Because of sequence similarities to the actin-binding site of a-actinin, the G.3.5 antigen is thought to be an a-actinin-like protein which may cross link actin to intermediate filaments (Price et al., 1993). In this study, we have compared the G.3.5 antigen isolated from bovine skeletal muscle with a smooth muscle isofonn of a-actinin using biochemical analysis and binding assays. We find that cytoplasmic a actinin and the G.3.5 antigen migrate similarly but not identically in a nonreducing environment When both antigens are subjected to partial proteolysis by the V8 protease, similar fragments are generated. Overlay-immunoblotting assays indicate that cytoplasmic a-actinin and the G.3.5 antigen bind filamentous actin and desmin simultaneously. On the other hand, analysis of the G.3.5 antigen by SDS-PAGE (12% separating/4% stacking) results in a 100 kDa 'doublet' band, which is further resolved into a 114 kDa single band and a 107 kDa doublet when separated by 7%/4% SDS-PAGE; cytoplasmic a-actinin produces only a single band (107 kDa by 7%/4% SDS-PAGE). Although the G.3.5 mAB and anti-cytoplasmic a-actinin mAB cross-react with each other's antigens, anti-sarcomeric a-actinin mAB does not recognize cytoplasmic a-actinin but does react with the G.3.5 antigen, therefore indicating differences in their immunorecognition. These findings support the hypothesis that the G.3.5 antigen is a novel isofonn of a-actinin with binding sites for both actin and desmin and serves to cross-link the two cytoskeletal fibers.