Document Detail


FTIR determination of ligand-induced secondary and tertiary structural changes in bovine plasminogen.
MedLine Citation:
PMID:  14649418     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human plasminogen undergoes a large tertiary structural change in the presence of lysine derivatives (e.g. epsilon-amino caproic acid, EACA). This change facilitates human plasminogen activation by human plasminogen activators, resulting in elevated blood plasmin levels. It is hypothesized that this structure-function relationship is similar for bovine plasminogen. The objectives of this study were to investigate the effect of the ligand EACA on the secondary structure of plasminogen (bovine, human, and rabbit) and the tertiary structure of bovine plasminogen using Fourier-transform infrared spectroscopy (FTIR). Spectra of plasminogen, EACA, and a mixture of plasminogen and EACA in water and deuterium were collected using FTIR. Fourier-self deconvoluted spectra in the amide I region (1700-1600 cm(-1)) were used to detect changes in secondary structure of plasminogen after EACA addition. Change in bovine plasminogen tertiary structure was determined by comparing ratios of amide II (1600-1500 cm(-1)) to amide I bond intensities over time for samples in deuterium. No differences in secondary structure were observed for any plasminogen in the presence of EACA; however, addition of EACA significantly changed tertiary structure of bovine plasminogen. This tertiary structural change indicates a transition from a folded to an unfolded state, which could be more easily converted to plasmin. These results are consistent with reported human plasminogen studies using neutron scattering (tertiary structure) and circular dichroism (secondary structure) methods.
Authors:
Kirby D Hayes; Banu F Ozen; S Suzanne Nielsen; Lisa J Mauer
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of dairy research     Volume:  70     ISSN:  0022-0299     ISO Abbreviation:  J. Dairy Res.     Publication Date:  2003 Nov 
Date Detail:
Created Date:  2003-11-27     Completed Date:  2004-03-08     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985125R     Medline TA:  J Dairy Res     Country:  England    
Other Details:
Languages:  eng     Pagination:  461-6     Citation Subset:  IM    
Affiliation:
Department of Food Science, Purdue University, 745 Agriculture Mall Drive, West Lafayette, IN 47907-1160, USA.
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MeSH Terms
Descriptor/Qualifier:
6-Aminocaproic Acid / pharmacology*
Animals
Antifibrinolytic Agents / pharmacology*
Cattle
Circular Dichroism
Female
Fibrinolysin / analysis,  chemistry
Humans
Ligands
Plasminogen / chemistry*,  drug effects,  physiology
Plasminogen Activators
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Rabbits
Spectroscopy, Fourier Transform Infrared / methods*
Structure-Activity Relationship
Chemical
Reg. No./Substance:
0/Antifibrinolytic Agents; 0/Ligands; 60-32-2/6-Aminocaproic Acid; 9001-91-6/Plasminogen; EC 3.4.21.-/Plasminogen Activators; EC 3.4.21.7/Fibrinolysin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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