Two-dimensional polyacrylamide gel electrophoresis analysis of cryoglobulins and identification of an IgM-associated peptide
Détails
ID Serval
serval:BIB_C9574665858C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Two-dimensional polyacrylamide gel electrophoresis analysis of cryoglobulins and identification of an IgM-associated peptide
Périodique
Journal of Immunological Methods
ISSN
0022-1759 (Print)
Statut éditorial
Publié
Date de publication
07/1994
Volume
173
Numéro
1
Pages
63-75
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jul 12
Research Support, Non-U.S. Gov't --- Old month value: Jul 12
Résumé
The clonality of immunoglobulins (Igs) in cryoprecipitates (n = 41) was studied by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). Our series included 24 cryoglobulins characterized by immunofixation electrophoresis (IF), 12 'trace amount' cryoglobulins, defined by a protein content in the precipitate of less than 0.05 mg/ml of serum, and five cryoglobulins of undetermined protein composition by IF. 2-D PAGE analysis showed polyclonal IgG associated either with monoclonal Igs (type II cryoglobulins; n = 14) or with polyclonal IgM (type III cryoglobulins; n = 14). In ten cryoprecipitates (two 'trace amount' cryoglobulins as well as seven of 19 type II and as one of five type III cryoglobulins by IF) polyclonal IgG were associated with a mixture of polyclonal and monoclonal IgM. These cryoglobulins were tentatively named type II-III cryoglobulins. A monoclonal IgM was observed in one cryoprecipitate (type I cryoglobulins). Two cryoglobulins presented unexpected 2-D patterns, characterized by the presence of oligoclonal IgM, with trace amounts of Igs of different isotypes (tentatively named type II-III(variant) cryoglobulins). A peptide of 44 kDa with a pI of 5.45 was observed in all cryoglobulins containing IgM (n = 40). This peptide was also present in purified monoclonal or polyclonal IgM fractions. N-terminal microsequencing (12 amino acid residues) revealed that this IgM-associated peptide was an unknown protein. Our results highlight the role of 2-D PAGE as an aid in the analysis of cryoglobulins.
Mots-clé
Amino Acid Sequence
Antibodies, Monoclonal/blood
Cryoglobulinemia/blood/immunology
Cryoglobulins/*analysis/classification
Electrophoresis, Gel, Two-Dimensional/*methods
Humans
Immunoglobulin Isotypes/blood
Immunoglobulin M/*blood
Isoelectric Point
Molecular Sequence Data
Molecular Weight
Peptides/*blood/chemistry/genetics
Pubmed
Web of science
Création de la notice
25/01/2008 15:34
Dernière modification de la notice
20/08/2019 15:44