Leann Pushee

Publication Date


Document Type


First Advisor

Johnson-Wint, Barbara

Degree Name

B.S. (Bachelor of Science)

Legacy Department

Department of Biological Sciences


Currently, no published study exists examining the effect of raised temperatures on Type 1 collagen fibril denaturation in a physiological environment. This study hypothesizes that some proportion of collagen in a physiological environment melts gradually as the temperature is increased above body temperature, and that the proportion will increase at a specific temperature with added time, until the rate of melting is slowed and a plateau is reached. This investigation will aid in a better understanding of how collagen reacts to any situation where the temperature of the connective tissue increases above normal. The temperatures measured were between 37°C (rat body temperature) and 45°C, at varying times from 0-2880 minutes. At specified times, aliquots of supernatant were drawn for analysis from a sample containing rat tail tendon collagen and complete supplement solution. Acid hydrolysis was performed and hydroxyproline assays were used to determine the amount of hydroxyproline in each sample. The hydroxyproline values were then converted into collagen amounts. In each case, aside from 44°C and 45 °C, a plateau was reached where the percentage of collagen denatured did not significantly increase. At 37°C and 38°C, there was little change of the percent denatured from start to finish. However, by 41°C, the melting occurring between 0 minutes and 240 minutes was significant. The only sample that completely melted was at 43°C. If given additional time, it appears that the 44°C and 45°C samples also would have fully denatured.


Includes bibliographical references.


9 unnumbered pages




Northern Illinois University

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