HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Swatland, H. J. Search for Related Content PubMed Articles by Swatland, H. J.

Fiber-Optic Reflectance and Autofluorescence of Bovine Elastin and Differences Between Intramuscular and Extramuscular Tendon¹

University of Guelph, Guelph, Ontario, Canada N1G 2W1

Abstract

A mercury illuminator, two monochromators and a photomultiplier were coupled with a bifurcated fiber-optic light guide to measure the reflectance and fluorescence of tendons and elastic ligaments from cattle. Tendons had a higher reflectance than ligamentum nuchae, particularly around 470 nm. However, the fluorescence emission spectra of tendons and ligamentum nuchae were very similar with a peak emittance from 440 nm (for extramuscular tendon and ligamentum nuchae) to 410 nm (for purified, freeze-dried Type I collagen and elastin fibers). The fluorescence emission spectrum of intramuscular tendon differed from that of extramuscular tendon. For intramuscular tendon, there was no peak in the 410- to 440-nm range and there was slightly higher emittance around 510 nm. A very similar pattern of divergence between emission spectra was also found for purified, freeze-dried collagen fibers derived from intramuscular tendon and for commercially available Type III vs Type I collagen. It was concluded that intramuscular tendon might have a higher proportion of Type III collagen than extramuscular tendon.

¹ Research supported by the Nat. Sci. and Eng. Res. Council of Canada and by the Ontario Ministry of Agr. and Food. Purified samples of collagen were kindly provided by Prof. R. O. Ball.

² Dept. of Anim. and Poul. Sci. and Dept. of Food Sci.