Open Access. Powered by Scholars. Published by Universities.®
Amino Acids, Peptides, and Proteins Commons™
Open Access. Powered by Scholars. Published by Universities.®
- Keyword
-
- Anemia, Hemolytic (1)
- Anti-citrullinated protein antibodies (ACPA) (1)
- Autoantibodies (1)
- Blood Proteins (1)
- Borohydrides (1)
-
- Diabetes (1)
- Diabetes Complications (1)
- Diabetes Mellitus (1)
- Diagnosis (1)
- Erythrocyte Membrane (1)
- Erythrocytes (1)
- Glycoproteins (1)
- Humans (1)
- IgG4 (1)
- In Vitro Techniques (1)
- Membrane Proteins (1)
- Nonenzymatic glycosylation (1)
- Pathogenesis (1)
- Proteins (1)
- Rheumatoid arthritis (1)
- Rheumatoid factor (RF) (1)
Articles 1 - 2 of 2
Full-Text Articles in Amino Acids, Peptides, and Proteins
Detection Of Igg4-Specific Autoantibodies In Rheumatoid Arthritis Serum Samples, Azra Borogovac, Youmna Lahoud, Janice Weaver, Sheldon M. Cooper, Mercedes Rincon, Jonathan Kay, Ellen M. Gravallese
Detection Of Igg4-Specific Autoantibodies In Rheumatoid Arthritis Serum Samples, Azra Borogovac, Youmna Lahoud, Janice Weaver, Sheldon M. Cooper, Mercedes Rincon, Jonathan Kay, Ellen M. Gravallese
Ellen M. Gravallese
Background: Rheumatoid arthritis (RA) is a chronic multi-system autoimmune disease characterized by inflammatory synovitis. Autoantibodies such as rheumatoid factor (RF) and anti-citrullinated protein antibodies (ACPA) have been implicated in the pathogenesis of RA, and are currently important criteria for diagnosis within the 2010 American College of Rheumatology (ACR)/European League Against Rheumatism (EULAR) classification criteria.1 Yet, many patients diagnosed with RA do not have measurable circulating ACPA or RF which may result in delayed diagnosis and treatment. After IgG1, IgG4 is the second most predominant isotype among ACPA and RF; however it is not detected in currently available diagnostic assays. Recent …
Nonenzymatic Glycosylation Of Erythrocyte Membrane Proteins. Relevance To Diabetes, J A. Miller, Ellen M. Gravallese, H F. Bunn
Nonenzymatic Glycosylation Of Erythrocyte Membrane Proteins. Relevance To Diabetes, J A. Miller, Ellen M. Gravallese, H F. Bunn
Ellen M. Gravallese
Nonenzymatic glycosylation of proteins of the erythrocyte membrane was determined by incubating erythrocyte ghosts with [3H]borohydride. The incorporation of tritium into protein provides a reliable assay of ketoamine linkages. The membrane proteins from 18 patients with diabetes incorporated twice as much radioactivity as membrane proteins from normal erythrocytes. After acid hydrolysis, amino acid analysis showed that the majority of radioactivity was localized to glucosyllysine. Autoradiograms showed that all of the major proteins of the erythrocyte membrane, separated by electrophoresis on sodium dodecyl sulfate gels, contained ketoamine linkages. No protein bands in either normal or diabetic erythrocytes showed significant preferential labeling. …