Fourier Transform Infrared Spectroscopy of Protein Adsorption from Whole Blood: II. Ex Vivo Sheep Studies
Authors: Winters, S.1; Gendreau, R.M.2; Leininger, R.I.2; Jakobsen, R.J.2
Source: Applied Spectroscopy, Volume 36, Issue 4, Pages 339-473 (July/August 1982) , pp. 404-409(6)
Publisher: Society for Applied Spectroscopy
Abstract:
The adsorption of proteins from ex vivo flowing sheep blood has been studied using FT-IR/ATR with spectra being collected at 0.8-s intervals of blood flow. We have found that protein adsorption can be divided into four adsorption regions: the first region being one of rapid adsorption of protein species such as albumin, an unknown protein species, glycoproteins, and some fibrinogen; in the second region, there is little increase in the total protein adsorbed, but there is evidence of protein replacement. Fibrinogen adsorption is the major event occurring in the third adsorption region, whereas the appearance of red blood cells and platelets marks the fourth region. Such knowledge of protein composition at various times in the adsorption process is providing molecular level information on thrombosis occurring on surfaces.Keywords: FT-IR; Protein absorption; Blood-surface interactions; Biocompatibility
Document Type: Research article
DOI: http://dx.doi.org/10.1366/0003702824639592
Affiliations: 1: Biological Spectroscopy Facility, Battelle-Columbus Laboratories, Columbus, Ohio 43201; present address: Department of Bioengineering, Merrill Hall, University of Utah, Salt Lake City, UT 84112 2: Biological Spectroscopy Facility, Battelle-Columbus, Laboratories, Columbus, Ohio 43201
Publication date: 1982-07-01
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- By this author: Winters, S. ; Gendreau, R.M. ; Leininger, R.I. ; Jakobsen, R.J.

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