Open AccessINTRAMOLECULAR LOCALIZATION OF THE ACCEPTOR CROSS-LINKING SITES IN FIBRIN
Author(s) -
L. Lóránd,
David M. Chenoweth
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.63.4.1247
Subject(s) - cyanogen bromide , chemistry , acceptor , fibrin , amine gas treating , intramolecular force , stereochemistry , reactivity (psychology) , photochemistry , biochemistry , organic chemistry , peptide sequence , biology , medicine , physics , alternative medicine , pathology , immunology , gene , condensed matter physics
Using 1-14 C-glycine ethyl ester to titrate and label the acceptor cross-linking sites in fibrin, it was possible to localize and characterize the reactivity of these sites. In terms of sulfitolyzed chain fragments, both α and γ chains were shown to act as amine-acceptors, the site in γ being more reactive. Identification and isolation of the acceptor loci were also achieved after cyanogen bromide fragmentation. It is interesting that the “N-terminal disulfide knot” portion of fibrin does not seem to contain acceptor functions.