Mouse myeloma proteins with lambda 2 and lambda 3 light chains.

T Cotner; K Blaser; J Kriedberg; M Potter; H N Eisen

Home/Archive/PubMed

PubMed · 6795267

Mouse myeloma proteins with lambda 2 and lambda 3 light chains.

T Cotner·K Blaser·J Kriedberg·M Potter·H N Eisen

View original source ↗Export metadata ↓

Abstract

Serum and ascites fluid from mice bearing 260 different myeloma tumors were screened serologically for myeloma proteins having light chains like that of L315, the lambda 2 chain produced by myeloma MOPC-315. Four proteins, made by myelomas TEPC-952, CBPC-49, ABPC-72, and SAPC-15, were identified. Their light chains were essentially indistinguishable serologically from L315, and each of them also yielded the characteristic C-terminal amino acid (leucine) and C-terminal tryptic peptide of L315. However, amino acid sequences and other findings reported elsewhere have revealed that although the light chain of TEPC-952 is indeed a lambda 2 chain, the light chains of the others (CBPC-49, ABPC-72, and SAPC-15) represent another, slightly different type of light chain, which has been designated lambda 3.

Explore related subjects

Amino Acids Animals Dinitrobenzenes Immune Sera Immunoglobulin Light Chains Immunoglobulin lambda-Chains Mice Mice, Inbred BALB C Myeloma Proteins Protein Binding Rabbits Trinitrobenzenes Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

T Cotner, K Blaser, J Kriedberg, M Potter, H N Eisen. 1981. Mouse myeloma proteins with lambda 2 and lambda 3 light chains.. https://pubmed.ncbi.nlm.nih.gov/6795267/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2026

Chimeric structural isomer fragments as cost-efficient internal standards for amino acid quantification by mass spectrometry.

Amino acid (AA) profiles from body fluids such as blood and urine are clinical indicators for diagnosing metabolic and hepatic diseases. Current quantitative methods, such as liquid chromatography-mass spectrometry (LC-MS) with isotopically labelled internal standards (ISs), are costly and technically demanding. This study proposes a cost-efficient alternative using structural isomers as ISs in a direct liquid infusion (DLI) tandem mass spectrometry (MS/MS) approach. The method leverages chimeric spectra and fragment intensity ratios to quantify AAs, demonstrating high linearity and precision even with a 3D ion trap mass analyser. This approach offers a viable strategy for AA quantification in preventive medicine, particularly for screening metabolic diseases such as phenylketonuria, diabetes, and liver dysfunction.

Amino Acids↗

PubMed1997

Serine/threonine kinase activity associated with the cytoplasmic domain of the lymphotoxin-beta receptor in HepG2 cells.

The lymphotoxin-beta receptor (LT-betaR) has been shown to be the receptor for the membrane-bound lymphotoxin heterotrimers LTalpha1/beta2 and LTalpha2/beta1. The extracellular domain of LT-betaR shows extensive similarity with members of the tumor necrosis factor receptor family, while its cytoplasmic domain is distinct and lacks any inherent enzymatic activity. This suggests that the interaction of LT-betaR with other molecules might be important for signal transduction. Here we demonstrate the association of a fusion protein, comprising glutathione S-transferase and the cytoplasmic domain of LT-betaR (GST-LT-betaR(CD)), with several proteins in the size range 29-80 kDa from HepG2 cell lysates. We present evidence that two of these proteins are serine/threonine kinases, which associate with amino acids 324-377 of the cytoplasmic domain of LT-betaR and phosphorylate this receptor. The characteristics of these novel kinases indicate that they are distinct from the previously described tumor necrosis factor receptor-associated kinases. This suggests the presence of novel signal transduction pathway(s) for LT-betaR.

Amino Acids↗

PubMed1997

Separation of 18 6-aminoquinolyl-carbamyl-amino acids by ion-pair chromatography.

Eighteen 6-aminoquinolyl-carbamyl (AQC)-amino acids were separated by ion-pair chromatography, using tetrabutylammonium (TBA) as a counterion. Optimum separation was obtained on a C8 reverse-phase column using gradient elution with two mobile phases, A (5 mM TBA, 75 mM ammonium acetate, pH 7.5) and B (80% acetonitrile). The AQC-amino acids were detected by fluorescence with excitation at 250 nm and emission at 395 nm, and the analysis time was 65 min. The response factors of individual AQC-amino acids to AQC-phenylalanine ranged from 0.42 to 1.08 (except for tryptophan at 0.01), with an average of 0.8. Detection limits by fluorescence ranged from 11.8 fmol (threonine) to 51.7 fmol (methionine), except for tryptophan (1.8 pmol).

Amino Acids↗