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Differential scanning calorimetry of albumin solders: Interspecies differences and fatty acid binding effects on protein denaturation
Author(s) -
Bleustein Clifford B.,
Sennett Michael,
Kung Robert T.V.,
Felsen Diane,
Poppas Dix P.,
Stewart Robert B.
Publication year - 2000
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 - 10.1002/1096-9101(2000)27:5<465::aid-lsm1007>3.0.co;2-s
Subject(s) - differential scanning calorimetry , denaturation (fissile materials) , enthalpy , chemistry , bovine serum albumin , albumin , fatty acid , calorimetry , serum albumin , chromatography , biochemistry , nuclear chemistry , thermodynamics , physics
Background and Objective Understanding albumin solder denaturation is important for laser tissue soldering. Human (HSA), bovine (BSA), porcine (PSA), and canine (CSA) albumin both fatty acid containing (FAC) and fatty acid free (FAF) were evaluated by using differential scanning calorimetry (DSC). Study Design/Materials and Methods DSC was used to measure difference thermograms to determine the irreversible thermal denaturation profile for 50% albumin solutions. The denaturation transition's onset, end and peak temperatures, and enthalpy were measured. Results All FAC species, except BSA, exhibited twin peaked endotherms. Single endotherms were observed for all FAF species and BSA‐FAC. Onset and end temperatures were significantly [ P < 0.001] lower for all FAF species (except BSA's end temperature). There was a 30% decrease in the denaturation enthalpy between FAF and FAC groups. Conclusion FAF albumin solders were found to denature at significantly lower temperatures, while also having a 30% reduction in enthalpy when compared with their FAC counterparts. Lasers Surg. Med. 27:465–470, 2000. © 2000 Wiley‐Liss, Inc.