Anshuman Swain1, Johannes Leisen2, Muhammad A. R. Anjum1, Joe Pearson3, Johnna S. Temenoff3, Felix M. Gonzalez1, and David A. Reiter1
1Department of Radiology and Imaging Sciences, Emory University, Atlanta, GA, United States, 2Department of Chemistry, Georgia Institute of Technology, Atlanta, GA, United States, 3Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, GA, United States
1Department of Radiology and Imaging Sciences, Emory University, Atlanta, GA, United States, 2Department of Chemistry, Georgia Institute of Technology, Atlanta, GA, United States, 3Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, GA, United States
HR-MAS 1H NMR data of ovine Achilles tendon and murine rotator cuff tendon reveals peaks attributed to non-collagenous matrix components such lactate, the SLRP family of proteoglycans, and lipids, and collagenous matrix components, such as proteins comprising the collagen fibrils.
Figure 2. HR-MAS 1H-NMR spectrum of ovine Achilles tendon recorded at 298K. Abbreviations used: Lac, Lactate; CS, Chondroitin sulfate; Lip, Lipids; Ile, Isolecuine; Leu, Leucine; Val, Valine; Glu, Glutamate; Pro, Proline; Asn, Asparagine; Hyp, Hydroxyproline; Gln, Glutamine.
Table 1. Chemical shift assignments of HR-MAS 1H-NMR spectra of ovine Achilles tendon and rat rotator cuff tendon. Abbreviations used: Lac, Lactate; CS, Chondroitin sulfate. All amino acids are labeled according to the three letter code.
