Our understanding of collagen has increased considerably. Collagen is a fibrous protein that plays a key role in the framework and development of hard and connective tissue. Collagen has vast structural possibilities for modifications to generate novel properties, functions, and applications especially in the bone implant arena. Collagen is found throughout nature in skin, tendon, bone, cartilage, etc. and in numerous different species. Of the 28 identified types, collagen I is the most abundant in nature and the main component of bone. Despite its abundance, the utilization and characterization has been restricted by its insolubility. Collagen solutions are usually viscous and difficult to study using techniques such as zeta potential analysis, chromatography and electrophoresis. The specific aim of this study was to develop a protocol to extract and solubilize collagen from chicken femur bone. In the thermogram of our chicken femur bone collagen (CBC), there was only a 35% reduction in weight. This signifies that the CBC collagen sample contained 65% inorganic material. Elemental analysis revealed that CBC consisted of 11% Carbon (C), 2% Hydrogen (H), and 3% Nitrogen (N), totaling 16%. This is substantially lower than 77%, the calculated theoretical value of CHN% in collagen. Our CBC shared the theoretical Carbon/Nitrogen value of 3.4. Elemental analysis confirms that the CBC contained elements other than carbon, nitrogen, and hydrogen. This suggests that the CBC sample was not fully demineralized and adjustments need to be made to the existing collagen extraction protocol. Further studies are needed to confirm chemical composition of the CBC in solution. This work is part of a larger study to compare collagen I, derived from bone, and α-chitin, derived from crab exoskeleton