DOI Seite / Zitierlink:
https://doi.org/10.11588/diglit.48120#0025
Abstracts
7
ing anti-P200 antibodies [7]. As these sera are both of high titer and affinity, they
provide a powerful tool for investigating the function of this protein.
References
1. Guilly, M-N. et al. (1987): Autoantibodies to nuclear lamin B in a patient with
thrombopenia. Eur. J. Cell Biol. 43, 266-272
2. Lassoued, K. et al. (1988): Antinuclear auto-antibodies specific for lamins. Annals
of Internal Medicine 108, 829-833
3. Cartaud, A. et al.: Presence of a protein immunologically related to lamin B in the
postsynaptic membrane of Torpedo marmorata electrocyte (submitted)
4. Lassoued, K. et al. (in preparation)
5. Lassoued, K. et al. (1988): Autoantibodies to 200 KD polypeptide(s) of the nuclear
envelope: a new serologic marker of primary biliary cirrhosis. Clin. Exp. Immunol. 74,
283-288
6. Courvalin, J-C. et al.: The 200 KD nuclear envelope polypeptide recognized by
human autoantibodies in Primary Biliary Cirrhosis is the major glycoprotein of the
pore complex (submitted)
7. Lassoued, K. et al.: (in preparation)
Cloned Human snRNP Proteins B and B' Differ Only in Their
Carboxy-Terminal Part
A. van Dam, I. Winkel, J. Zijstra-Baalbergen, R. Smeenk and H.T. Cuypers
Central Laboratory of the Red Cross Blood Transfusion Service, Plesmanlaan 125,
1066 CX Amsterdam, The Netherlands
Autoantibodies against the snRNP proteins B and B' are a common feature
of the autoimmune disease systemic lupus erythematosus [1]. We screened a
Agtl 1 cDNA expression library, made from polyA+ RNA from HL-60 cells, with
a monoclonal antibody specific for B and B'. This monoclonal antibody was ob-
tained from a fusion between spleen cells of an MRL/lpr mouse and sp2/0 cells.
Screening of 700000 clones resulted in three positive clones (clone 5, 9 and 16),
which reacted also with a second monoclonal antibody specific for B and B' and
with a panel of human anti-B/B' sera, obtained from patients with autoimmune
diseases.
To characterize ^-galactosidase fusion proteins, clone 5, 9 and 16 were in-
troduced in a lysogenic host. All three clones produced fusion proteins with a mo-
7
ing anti-P200 antibodies [7]. As these sera are both of high titer and affinity, they
provide a powerful tool for investigating the function of this protein.
References
1. Guilly, M-N. et al. (1987): Autoantibodies to nuclear lamin B in a patient with
thrombopenia. Eur. J. Cell Biol. 43, 266-272
2. Lassoued, K. et al. (1988): Antinuclear auto-antibodies specific for lamins. Annals
of Internal Medicine 108, 829-833
3. Cartaud, A. et al.: Presence of a protein immunologically related to lamin B in the
postsynaptic membrane of Torpedo marmorata electrocyte (submitted)
4. Lassoued, K. et al. (in preparation)
5. Lassoued, K. et al. (1988): Autoantibodies to 200 KD polypeptide(s) of the nuclear
envelope: a new serologic marker of primary biliary cirrhosis. Clin. Exp. Immunol. 74,
283-288
6. Courvalin, J-C. et al.: The 200 KD nuclear envelope polypeptide recognized by
human autoantibodies in Primary Biliary Cirrhosis is the major glycoprotein of the
pore complex (submitted)
7. Lassoued, K. et al.: (in preparation)
Cloned Human snRNP Proteins B and B' Differ Only in Their
Carboxy-Terminal Part
A. van Dam, I. Winkel, J. Zijstra-Baalbergen, R. Smeenk and H.T. Cuypers
Central Laboratory of the Red Cross Blood Transfusion Service, Plesmanlaan 125,
1066 CX Amsterdam, The Netherlands
Autoantibodies against the snRNP proteins B and B' are a common feature
of the autoimmune disease systemic lupus erythematosus [1]. We screened a
Agtl 1 cDNA expression library, made from polyA+ RNA from HL-60 cells, with
a monoclonal antibody specific for B and B'. This monoclonal antibody was ob-
tained from a fusion between spleen cells of an MRL/lpr mouse and sp2/0 cells.
Screening of 700000 clones resulted in three positive clones (clone 5, 9 and 16),
which reacted also with a second monoclonal antibody specific for B and B' and
with a panel of human anti-B/B' sera, obtained from patients with autoimmune
diseases.
To characterize ^-galactosidase fusion proteins, clone 5, 9 and 16 were in-
troduced in a lysogenic host. All three clones produced fusion proteins with a mo-