Faculty and Staff

In spring 2013, the presenters developed a survey on academic library streaming video and distributed it broadly through various discussion and mailing lists.

This is the first large-scale and most comprehensive effort to date to collect data on streaming video funding, licensing, acquisition, and hosting in academic libraries. Its results will provide benchmark data for future explorations of this rapidly expanding approach to video in academic libraries.

Streaming video is becoming a common occurrence on many campuses today. Its fast growth is due in part to the steady growth of online classes and programs. Technology has also played a role in this growth as alternatives for ingesting and accessing content have expanded. Multiple options are now available including in-house approaches, cloud storage, and third party vendors.

This survey collected data on how academic institutions address the day-to-day operations related to streaming video as well as perceived directions for future action.

Survey questions addressed selection and acquisition of video in both hard copy and streaming formats, funding for acquisitions, current and planned hosting interfaces, cataloging and access, and current practice and policy on digitization of hard copy titles for streaming. This session reviews the instrument used, and provides a preliminary look at some of the key data collected.

We sought to evaluate the reproducibility of a liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based approach to measure the stable-isotope enrichment of in vivo-labeled muscle ATP synthase β subunit (β-F1-ATPase), a protein most directly involved in ATP production, and whose abundance is reduced under a variety of circumstances. Muscle was obtained from a rat infused with stable-isotope-labeled leucine. The muscle was homogenized, β-F1-ATPase immunoprecipitated, and the protein was resolved using 1D-SDS PAGE. Following trypsin digestion of the isolated protein, the resultant peptide mixtures were subjected to analysis by HPLC-ESI-MS/MS, which resulted in the detection of multiple β-F1-ATPase peptides. There were three β-F1-ATPase unique peptides with a leucine residue in the amino acid sequence, and which were detected with high intensity relative to other peptides and assigned with >95% probability to β-F1-ATPase. These peptides were specifically targeted for fragmentation to access their stable-isotope enrichment based on MS/MS peak areas calculated from extracted ion chromatographs for selected labeled and unlabeled fragment ions. Results showed best linearity (R[superscript 2] = 0.99) in the detection of MS/MS peak areas for both labeled and unlabeled fragment ions, over a wide range of amounts of injected protein, specifically for the β-F1-ATPase[subscript 134-143] peptide. Measured stable-isotope enrichment was highly reproducible for the β-F1-ATPase[subscript 134-143] peptide (CV = 2.9%). Further, using mixtures of synthetic labeled and unlabeled peptides we determined that there is an excellent linear relationship (R[superscript 2] = 0.99) between measured and predicted enrichment for percent enrichments ranging between 0.009% and 8.185% for the β-F1-ATPase[subscript 134-143] peptide. The described approach provides a reliable approach to measure the stable-isotope enrichment of in-vivo-labeled muscle β-F1-ATPase based on the determination of the enrichment of the β-F1-ATPase[subscript 134-143] peptide.