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PMID: 4530289 Published · ppublish English Journal Article

Conformation of fibrinogen: calorimetric evidence for a three-nodular structure.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 71 ·No. 10 ·1974-10-00 ·Pages 4125-8

Donovan JW, Mihalyi E

Abstract

Solutions of fibrinogen show two endothermal (denaturing) transitions, at 61 degrees and at 100 degrees , when heated in a differential scanning calorimeter. Similar transitions are observed for a mixture of the fragments D and E obtained by limited proteolysis of fibrinogen. Isolated fragment E shows only a single transition, at 97 degrees . The independent thermal denaturation of these portions of fibrinogen supports the three-nodular model proposed for fibrinogen. The D and E subunits retain their characteristic denaturation behavior when fibrinogen is clotted by thrombin addition, but over a period of about one hundred times the clotting time, the denaturation temperature of the D subunit increases by 9 degrees and its enthalpy of denaturation by one-third. Since this change takes place in the absence of Factor XIII activity, and its rate is proportional to thrombin concentration, it is presumed to be mediated by a proteolytic cleavage distinct from those which liberate the A and B fibrinopeptides.

MeSH Terms
Animals Calorimetry Cattle Fibrinogen Hot Temperature Hydrolysis Peptide Fragments/analysis Protein Conformation Protein Denaturation Trypsin
Chemicals
Peptide Fragments Fibrinogen Trypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Donovan J W
Mihalyi E
References (20)
20 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.71.10.4125
Published
1974-10-00
Pages
4125-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC434341
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.71.10.4125 PMC Full Text View journal details
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