Abstract
Human factor V was subjected to desialation and deglycosylation to investigate the function of the molecular carbohydrate moiety. Removal of 90% of the sialic acid residues resulted in a 1.5–2‐fold increase in clotting activity, and up to 70% deglycosylation in a concurrent decrease in clotting activity. Desialation had no effect on thrombin‐induced activation, whereas deglycosylated factor V activation was impaired. Lectin‐blot experiments with sialic‐acid‐specific Limax flavus agglutinin (LFA), galactose‐specific Ricinus communis agglutinin (RCA‐II) and mannose‐specific concanavalin A on thrombin‐induced factor V fragments revealed the presence of carbohydrate residues in fragments B, C1, D and F1F2. Interestingly, sialic acid was present in C1 whilst galactose was not detectable. Fragment F1 F2 contained terminal galactose residues. LFA and RCA‐II inhibited the procoagulant activity of native factor V and of desialated factor V respectively. These investigations distinctly indicate the important role of the human factor V carbohydrate moiety in the process of blood coagulation.
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Dates
Type | When |
---|---|
Created | 20 years, 5 months ago (March 3, 2005, 8:52 p.m.) |
Deposited | 1 year, 11 months ago (Aug. 30, 2023, 3:51 p.m.) |
Indexed | 1 year, 9 months ago (Oct. 28, 2023, 1:46 a.m.) |
Issued | 37 years, 8 months ago (Dec. 1, 1987) |
Published | 37 years, 8 months ago (Dec. 1, 1987) |
Published Online | 20 years, 5 months ago (March 3, 2005) |
Published Print | 37 years, 8 months ago (Dec. 1, 1987) |
@article{BRUIN_1987, title={The function of the human factor V carbohydrate moiety in blood coagulation}, volume={170}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1987.tb13700.x}, DOI={10.1111/j.1432-1033.1987.tb13700.x}, number={1–2}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={BRUIN, Taco and STURK, Augueste and TEN CATE, Jan W. and CATH, Marieke}, year={1987}, month=dec, pages={305–310} }