Freeing sodium thiocyanate from iron in the manufacture of nitron fibre

1981 ◽  
Vol 12 (6) ◽  
pp. 379-381
Author(s):  
N. M. Savel'eva ◽  
M. G. Bol'shakova ◽  
L. B. Yakushkin
Keyword(s):  
Sodium Thiocyanate ◽  
Nitron Fibre

Extraction purification of the sodium thiocyanate in nitron fibre production

1978 ◽  
Vol 9 (5) ◽  
pp. 499-502
Author(s):  
M. G. Bol'shakova ◽  
G. M. Mikheeva ◽  
A. �. Fridberg ◽  
L. B. Yakushkin ◽  
G. M. Sitnikov
Keyword(s):  
Fibre Production ◽  
Sodium Thiocyanate ◽  
Nitron Fibre

Iron extraction from the sodium thiocyanate liquors in nitron fibre production

1975 ◽  
Vol 6 (3) ◽  
pp. 321-323
Author(s):  
I. S. Rabinovich ◽  
L. P. Khomutova
Keyword(s):  
Fibre Production ◽  
Sodium Thiocyanate ◽  
Nitron Fibre ◽  
Iron Extraction

Thermal properties of poly(ethylene oxide) complexed with sodium thiocyanate and potassium thiocyanate

1987 ◽  
Vol 20 (12) ◽  
pp. 3023-3034 ◽  
Author(s):  
C. Robitaille ◽  
S. Marques ◽  
D. Boils ◽  
J. Prud'homme
Keyword(s):  
Thermal Properties ◽  
Ethylene Oxide ◽  
Potassium Thiocyanate ◽  
Sodium Thiocyanate ◽  
Poly Ethylene Oxide ◽  
Poly Ethylene

scholarly journals Studies of mammalian ornithine decarboxylase using a monoclonal antibody

1984 ◽  
Vol 217 (1) ◽  
pp. 123-128 ◽  
Author(s):  
A E Pegg ◽  
J E Seely ◽  
L Persson ◽  
M Herlyn ◽  
K Ponsell ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Ornithine Decarboxylase ◽  
Mouse Kidney ◽  
Immunoglobulin M ◽  
Active Enzyme ◽  
Sodium Thiocyanate ◽  
Immunoaffinity Column ◽  
Rapid Turnover ◽  
Cytosolic Protein

A monoclonal antibody of the immunoglobulin M class was produced against mouse kidney ornithine decarboxylase. Screening for the antibody was carried out using alpha-difluoromethyl[5-3H]ornithine-labelled ornithine decarboxylase. The antibody reacted with this antigen and with native ornithine decarboxylase. The antibody attached to Sepharose could be used to form an immunoaffinity column that retained mammalian ornithine decarboxylase. The active enzyme could then be eluted in a highly purified form by 1.0M-sodium thiocyanate. The monoclonal antibody could also be used to precipitate labelled ornithine decarboxylase from homogenates of kidneys from androgen-treated mice given [35S]methionine. Only one band, corresponding to Mr of about 55000, was observed. The extensive labelling of this band is consistent with the rapid turnover of ornithine decarboxylase protein, since this enzyme represents only about 1 part in 10000 of the cytosolic protein.

scholarly journals Bacteriolysis of Streptococcus mutans GS5 by lysozyme, proteases, and sodium thiocyanate.

1982 ◽  
Vol 38 (3) ◽  
pp. 1172-1180 ◽  
Author(s):  
T J Wilkens ◽  
H Goodman ◽  
B J MacKay ◽  
V J Iacono ◽  
J J Pollock
Keyword(s):  
Streptococcus Mutans ◽  
Sodium Thiocyanate

Hierarchy in the Avidity and Cross-reactivity of Anti-citrullinated Protein Antibodies in the Serum of Patients With Rheumatoid Arthritis

2020 ◽  
Author(s):  
Akihisa Haraguchi ◽  
Hisakata Yamada ◽  
Takahide Sakuragi ◽  
Tomomi Tsuru ◽  
Masakazu Kondo ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Immune Response ◽  
Serum Antibody ◽  
Cross Reactivity ◽  
Sodium Thiocyanate ◽  
Fine Specificity ◽  
Thiocyanate Solution ◽  
Citrullinated Protein ◽  
Citrullinated Peptide ◽  
Substantial Extent

Abstract BackgroundFine specificity of anti-citrullinated protein antibodies (ACPAs), in which cross-reactivity exists, varies among patients with rheumatoid arthritis (RA), but it is unclear whether the mechanism of ACPA production is same or different among individuals. Since avidity of serum antibody reflects the direction of immune response, we compared the levels of avidity and cross-reactivity between various ACPAs in a cohort of RA patient.MethodsSera from 180 RA patients positive for anti-cyclic citrullinated peptide (CCP) 2 antibody were screened for positivity of antibodies against CCP1, and citrullnated fibrinogen (cFib), enolase (cEno), and vimentin (cVim) peptides. Avidity of the four ACPAs, and some autoantibodies and antibodies against foreign antigens was determined by an elution assay using sodium thiocyanate solution. Cross-reactivity between different ACPAs was estimated by measuring the inhibition of binding by competitor peptides. ResultsThe prevalence of anti-CCP1, anti-cFib, anti-cEno, and anti-cVim antibodies in the anti-CCP2-positive RA cohort were 37.7%, 38.3%, 15.6%, and 23.9%, respectively. The avidity of ACPAs, except for anti-cVim antibody, was significantly lower than that of antibodies against foreign antigens, while there was a large variety in the avidity of other autoantibodies. At individual levels, the avidity of anti-cVim was significantly higher than that of other ACPAs, and there was a significant correlation in the avidity of anti-CCP and anti-cFib antibodies. Substantial extent of cross-reactivity was seen between different ACPAs, which also showed a fixed hierarchy.ConclusionThe fixed hierarchy in the avidity and cross-reactivity between different ACPAs suggests that the mechanism underlying ACPA production is common to all RA patients. Presence of a dominant antigen that induces whole ACPA response is speculated.

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