Preparation and characterization of NH2-terminal fibrinogen B beta fragments from N-DSK of human fibrinogen.
In order to investigate the early release of NH2-terminal plasmic fragments from the B beta chain of fibrinogen, substantial quantities of B beta 1-42 and B beta 1-21 are required as immunogens, as radioimmunoassay standards and for infusion into human volunteers to determine the half-lives of these peptides. Towards this end methods that employ selective proteolytic cleavage of these fragments from fibrinogen have been developed. Both the N-DSK fragment, produced by CNBr cleavage of fibrinogen, and B beta 1-118 were employed as substrates for plasmin with the finding of higher yields from N-DSK. B beta 1-42 and B beta 1-21 were purified by gel filtration and ion-exchange chromatography on SP-Sephadex using volatile buffers. When the purified preparation of B beta 1-42 was chromatographed on reverse-phase high performance liquid chromatography, two peaks of identical amino acid composition were separated, presumably due either to pyroglutamate or to amide differences.
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003488:Cyanogen Bromide; D005338:Fibrin Fibrinogen Degradation Products / Q000032:analysis* / Q000302:isolation & purification*; D005341:Fibrinolysin / Q000378:metabolism; D006801:Humans; D008722:Methods; D010446:Peptide Fragments; D013997:Time Factors
D005338:Fibrin Fibrinogen Degradation Products; D010446:Peptide Fragments; C041264:amino-terminal disulfide knot; C035285:fibrinogen Bbeta (1-42); C041263:fibrinogen Bbeta (1-21); D005341:Fibrinolysin; D003488:Cyanogen Bromide