title: Non-covalent associations of proteins in plasma: self-, mixed fibrin(ogen), mixed protein-non-protein associations.
abstract: OBJECTIVE
  To review biochemical literature and determine the significance of non-covalent bonding in plasma.
  
  
  RESULTS
  Many non-covalent bonds exist in plasma. Relatively strong self-associations are found for serum albumin, several gamma-globulins, apolipoproteins and fibrin(ogen). Here, fibrinogen and fibrin, considered one specie, react with other blood entities, building structures in plasma. A surface phenomenon analogous to viscosity is described for fibrin(ogen) which is useful in studying bonding. Combinations of lipids, proteins, polysaccharides and cellular elements form mixed associations. They add to the variety and number of non-covalent associations of proteins. Lipids make fairly strong associations.
  
  
  CONCLUSIONS
  Fibrinogen binding may play a major role in organizing blood to develop primitive structure. Lipids too may add to forming large structures. Non-covalent bonds are very common in plasma, and blood may have to be considered as a quasi-structured tissue.
authors.affiliation: Department of Pathology, State University of New York, Health Science Center at Brooklyn 11203, USA.
authors.forename: M
authors.initials: M
authors.lastname: London
mesh_terms: D001053:Apolipoproteins / Q000097:blood / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism*; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D010958:Plasminogen / Q000378:metabolism*; D011485:Protein Binding; D005719:gamma-Globulins / Q000378:metabolism*
chemical_list: D001053:Apolipoproteins; D001798:Blood Proteins; D005719:gamma-Globulins; D005337:Fibrin; D005340:Fibrinogen; D010958:Plasminogen