Premium
Quantitative measurements of linear birefringence during heating of native collagen
Author(s) -
Maitland Duncan J.,
Walsh Joseph T.
Publication year - 1997
Publication title -
lasers in surgery and medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.888
H-Index - 112
eISSN - 1096-9101
pISSN - 0196-8092
DOI - 10.1002/(sici)1096-9101(1997)20:3<310::aid-lsm10>3.0.co;2-h
Subject(s) - birefringence , arrhenius equation , materials science , anisotropy , activation energy , kinetic energy , enthalpy , chemistry , analytical chemistry (journal) , optics , thermodynamics , physics , chromatography , quantum mechanics
Background and Objective Linear birefringence is an anisotropic property of rat tail tendon, which is largely composed of collagen. Our goal is to show that the dynamic range and sensitivity of the linear birefringence loss of collagen during heating are sufficient for kinetic modeling of the reaction. Study Design/ Materials and Methods: The linear birefringence loss was quantified for tendon denatured via both a heated‐isotonic‐saline bath and a heated stage. All measurements were made with a polarizing transmission microscope equipped with a Berek compensator. Results The data show that the loss of linear birefringence is a first‐order kinetic reaction. The native rat tail tendon birefringence, Δn = 3.0 ± 0.6 × 10 −3 (mean ± std. err.), is lost after denaturation occurs (Δn = 0). Application of the Arrhenius equation to the linear birefringence data yields the activation energy (E a = 89 ± 1 kcal/mole), pre‐exponential coefficient (A = e 130±1 s −1 ), enthalpy (ΔH = 88 ± 1 kcal/mole) and entropy (ΔS = 197 ± 2 cal/°K·mole). Conclusion This study shows that dynamic changes in linear birefringence can be used to monitor thermally induced changes in collagen. Lasers Surg. Medicine 20:310–318, 1997. © 1997 Wiley‐Liss, Inc.