A single-step purification procedure and partial amino acid sequence analysis of picomole amounts of the rat T cell alloantigen RT6.2.
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Summary
A single-step immunoaffinity purification procedure for the rat T cell marker RT6.2 is described which permits the isolation of microgram quantities of protein from the RT 6.2+ T-T hybridoma EpD3.2 and revealed no significant homology to other proteins.
- Type
- article
- Published
- 1989-12-01
- Cited by
- 8
- References
- 10
- OpenAlex
- https://openalex.org/W2632369
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:40315954
Keywords
Computer science, Learning Management, Psychology, Multimedia
References
- The rat T-cell differentiation marker RT6.1 is more polymorphic than its alloantigenic counterpart RT6.2.
- A one-step purification of membrane proteins using a high efficiency immunomatrix.
- Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system.
- Absence of the RT-6 T cell subset in diabetes-prone BB/W rats.
- Production of a Rat T Cell Hybridoma That Stably Expresses the T Cell Differentiation Marker RT6.2
- Integrins: a family of cell surface receptors.
- The immunoglobulin superfamily--domains for cell surface recognition.
- Beyond transcriptional events
- Release of the rat T cell alloantigen RT-6.2 from cell membranes by phosphatidylinositol-specific phospholipase C
- Biochemical characterization of the T-cell alloantigen RT-6.2.
- Measurement, Design, and Analysis: An Integrated Approach.
Cited by
- Mouse T Cell Membrane Proteins Rt61 and Rt62 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Secondary Structure Motifs with ADP-ribosylating Bacterial Toxins (*)
- Purification and PCR-based cDNA cloning of a plastidial n-6 desaturase
- The erythrocyte receptor for the channel‐forming toxin aerolysin is a novel glycosylphosphatidylinositol‐anchored protein
- Purification and cDNA sequencing of an oleate-selective acyl-ACP:sn-glycerol-3-phosphate acyltransferase from pea chloroplasts
- Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat.
- A cytochrome-b5-containing fusion protein similar to plant acyl lipid desaturases.
- Increase in ADP‐ribosyltransferase activity of rat T lymphocyte alloantigen RT6.1 by a single amino acid mutation
- NAD+-dependent ADP-ribosylation of T Lymphocyte Alloantigen RT6.1 Reversibly Proceeding in Intact Rat Lymphocytes (*)
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