Deglycosylated prothrombin fragment 1. Calcium binding, phospholipid interaction, and self-assocation.

C. H. Pletcher, R. M. Resnick, G. J. Wei, V. A. Bloomfield, G. L. Nelsestuen

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


The carbohydrate portion of prothrombin fragment 1 has been removed by fluorolysis in anhydrous HF. The deglycosylated protein retains its calcium- and membrane-binding properties. The slow, calcium-dependent protein transition monitored by changes in intrinsic protein fluorescence remains intact for the aglycoprotein. Calcium-dependent protein-membrane binding is also observed and can be quantitatively reversed with EDTA. The major alteration resulting from carbohydrate removal is the degree of protein self-association. Both the normal and deglycosylated proteins undergo a rapid self-association which approaches a dimer in the presence of calcium. This self-association is independent of the slow change in intrinsic fluorescence. The deglycosylated protein then undergoes a secondary self-association with kinetics identical with the fluorescence change. This secondary self-association also occurs on the membrane surface. This suggests that the calcium-dependent conformational change exposes a site on the protein which functions in secondary self-association. The carbohydrate apparently masks this site in the native molecule.

Original languageEnglish (US)
Pages (from-to)7433-7438
Number of pages6
JournalJournal of Biological Chemistry
Issue number15
StatePublished - Aug 10 1980
Externally publishedYes


Dive into the research topics of 'Deglycosylated prothrombin fragment 1. Calcium binding, phospholipid interaction, and self-assocation.'. Together they form a unique fingerprint.

Cite this