The formation of beta fibrin requires a functional a site.
We used recombinant fibrinogens in which the a site is disrupted to examine beta-fibrin formation in the absence of a functional a site. Our variants have only b sites available, and they showed no evidence of fibrin polymer formation after cleavage of FpB with venzyme. We conclude that B-b interactions are not strong enough to induce clot formation. Our studies do not rule out the involvement of b in the formation of beta-fibrin, yet they do provide evidence that a is likely to be essential in the formation of beta-fibrin.
Hogan
K A
KA
Department of Pathology and Laboratory Medicine, University of North Carolina, Brinkhaus-Bullitt 603, Chapel Hill, NC 27599-7525, USA.
Bolliger
B
B
Okumura
N
N
Lord
S T
ST
D005337:Fibrin / Q000096:biosynthesis* / Q000378:metabolism; D005340:Fibrinogen / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D011994:Recombinant Proteins; D005337:Fibrin; D005340:Fibrinogen