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Nejvíce citované: 13608526

12 citací v PubMed Filtry

Nejvíce citovaný článek - PubMed ID 13608526

Nase zkusenosti mikromodifikací imunoelektroforesy
[Our experience with a micromodification of immunoelectrophoresis]

Ceskoslovenska epidemiologie, mikrobiologie, imunologie. 1958 Nov ; 7 (6) : 414-7.

Cesk Epidemiol Mikrobiol Imunol
ISSN 0009-0522
Zdroj

Článek

The gamma 1 heavy-chain disease FOR protein is present in two molecular forms

Folia microbiologica. 1984 ; 29 (3) : 254-63.

Folia Microbiol (Praha)
ISSN 0015-5632
Zdroj

Heavy chain disease proteins (FOR) were isolated from human plasma. These proteins were also detected immunochemically in the urine of the patient. The proteins were disulphide-linked Fc-like dimers with molar mass 64.2 kg/mol and sedimentation rate S020,W = 0.356 ps (3.56 S). Similar amounts of aspartic acid and pyroglutamic acid were found at the N-terminus. After cyanogen bromide cleavage of the FOR proteins, three peptides were isolated and their amino acid composition and partial amino acid sequence was determined. We suggest that two Fc-like proteins of similar sizes are present in the plasma: (1) the first with N-terminal aspartic acid corresponding to position 221 of gamma 1 EU chain and (2) the second with N-terminal pyroglutamic acid. The first protein and small amounts of related low-molar mass fragments found also in the plasma could be degradation products of the second protein. Evidence is given on structural differences between the FOR proteins and the corresponding portion of the gamma 1 EU chain.

MeSH
imunoglobuliny - gama-řetězce izolace a purifikace MeSH
lidé MeSH
nemoc z těžkých řetězců MeSH
sekvence aminokyselin MeSH
těžké řetězce imunoglobulinů izolace a purifikace MeSH
Check Tag
lidé MeSH
Publikační typ
časopisecké články MeSH
Názvy látek
FOR heavy chain disease protein, human MeSH Prohlížeč
heavy chain disease proteins, human MeSH Prohlížeč
imunoglobuliny - gama-řetězce MeSH
těžké řetězce imunoglobulinů MeSH

Článek

Interactions of pig Fab gamma fragments with protein A from Staphylococcus aureus

Zikán, J
Autor Zikán, J

Folia microbiologica. 1980 ; 25 (3) : 246-53.

Folia Microbiol (Praha)
ISSN 0015-5632
Zdroj

Ninety % of pig serum IgG was bound to protein A-Sepharose. Both individual fractions of the IgG, separated on the basis of their electric charge, were adsorbed on protein A-Sepharose to a similar extent. However, these fractions differed in their elution profile from the protein A-Sepharose when a gradient of increasing molarity of MgCl2 was used. Relative amounts of fractions eluted in higher concentrations of MgCl2 were augmented with the increasing amount of IgG bound to SpA-Sepharose. Not only high proportions of Fc fragments, but also nearly half of Fab fragments reacted with protein A. This latter interaction, confirmed also by affinity electrophoresis, did not have the character of a specific reaction of antibody with antigen.