PROTEIN PRESERVATION IN CASTOROIDES OHIOENSIS FROM NEW YORK

Molecular preservation in bone has been shown to decrease after excavation and storage in museums; however, few studies have examined the preservation of proteins in historically collected specimens. Recent interest has expanded on Pleistocene taxa from New York state to better understand and constrain geologic ages of these specimens collected in the nineteenth century. Specifically, a specimen of Castoroides ohioensis (NYSM VP-47; 10,150 ± 50 ¹⁴C BP), collected in 1845, represents the second specimen and first skull of this species collected and described. NYSM VP-47 was collected from a fine sand layer below a layer of peat, a typical depositional environment for fossils of this age in New York. Because of its histological significance, we wanted to investigate protein preservation within the skull using high-resolution mass spectrometry to expand our understanding of this taxon beyond basic morphological information and begin understanding retention of proteins in historically collected specimens. Using fragments of the nasal turbinates, we extracted proteins using methodology developed in our laboratory and analyzed them using an Orbitrap XL mass spectrometer after separation on an Agilent 1200 series HPLC. We were able to detect peptides from both collagen alpha chains supporting that a historically collected specimens can still provide critical molecular information. This study also represents the first use of mass spectrometry on Pleistocene taxa from the northeastern United States, and the first study to characterize collagen I sequences from Castoroides ohioensis.