scholarly journals On the Nature of the Yeast Phenylalanine Transfer Ribonucleic Acid Synthetase Recognition Site

1970 ◽  
Vol 245 (9) ◽  
pp. 2465-2468
Author(s):  
Bernard S. Dudock ◽  
Claudia DiPeri ◽  
Miriam S. Michael
1997 ◽  
Vol 77 (04) ◽  
pp. 760-766 ◽  
Author(s):  
Hiroshi Mohri ◽  
Etsuko Yamazaki ◽  
Zekou Suzuki ◽  
Toshikuni Takano ◽  
Shumpei Yokota ◽  
...  

SummaryA 20-year-old man with severe von Willebrand disease recently presented a progressive bleeding tendency, characterized recurrent subcutaneous hemorrhages and cerebral hemorrhage. Mixing and infusion studies suggested the presence of an inhibitor directed against vWF:RCo activity of von Willebrand factor (vWF) without significant inhibition of the FVIII:C. The inhibitor was identified as an antibody of IgG class. The inhibitor inhibited the interaction of vWF in the presence of ristocetin and that of asialo-vWF with GPIb while it partially blocked botrocetin-mediated interaction of vWF to GPIb. The inhibitor reacted with native vWF, the 39/34kDa fragment (amino acids [aa] 480/ 481-718) and the recombinant vWF fragment (MalE-rvWF508-704), but not with Fragment III-T2 (heavy chains, aa 273-511; light chains, aa 674-728). A synthetic peptide (aa 514-542) did not inhibit vWF-inhibitor complex formation. We conclude that this is the first autoantibody of class IgG from human origin that recognizes the sequence in the A1 loop of vWF, resulting in a virtual absence of functional vWF and a concomitant severe bleeding tendency although recognition site is different from the residues 514-542 which is crucial for vWF-GPIb interaction.


1967 ◽  
Vol 1 (6) ◽  
pp. 1271-1273 ◽  
Author(s):  
Y C Zee ◽  
L Talens ◽  
A J Hackett
Keyword(s):  

1986 ◽  
Vol 50 (4) ◽  
pp. 428-451
Author(s):  
T C King ◽  
R Sirdeskmukh ◽  
D Schlessinger
Keyword(s):  

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