Isolation and chemical characterization of the human B29 and mb-1 proteins of the B cell antigen receptor complex

Molecular Immunology
S VasileB K Seon

Abstract

A disulfide-linked heterodimeric antigen from human B leukemia cells was detected by radioimmunoprecipitation and Western blot analysis using a monoclonal antibody (mAb). The mAb was generated against a cell membrane antigen preparation from human B prolymphocytic leukemia cells and found to define an extracellular epitope of the smaller component (beta chain) of a heterodimeric antigen on human B leukemia cells. The antigen from BALL-1, a human B leukemia cell line, and fresh (uncultured) B prolymphocytic leukemia cells was found to consist of a 44-49 kDa (alpha chain) and a 36-40 kDa (beta chain) component. An additional minor component of 34 kDa was detected in the reduced antigen from BALL-1. For chemical identification of the antigen, we isolated the antigen from a Triton X-100 lysate of BALL-1 by immunoaffinity chromatography using the mAb. Determination of the amino-terminal amino acid sequences of the alpha and beta chains unequivocally identified them as the human mb-1 and B29 proteins, respectively. The sequence analyses indicate the molecular heterogeneity of the mb-1 protein and also perhaps the heterogeneity of the B29 protein. We detected three forms of the mb-1 protein which share an identical amino-terminal amin...Continue Reading

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Citations

Sep 19, 2009·Immunologic Research·Ben K SeonHilda Tsai
Apr 9, 2015·Frontiers in Pharmacology·Salma Y Abo ElnazarAmira M Abouelella
Mar 31, 2009·Biochimica Et Biophysica Acta·J Wolff
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May 10, 2018·FEBS Letters·Zhongyu ZhangGuihua Tai
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Jul 24, 2020·Expert Opinion on Investigational Drugs·Estelle Bourbon, Gilles Salles
Jun 9, 2001·Applied Immunohistochemistry & Molecular Morphology : AIMM·P G Chu, D A Arber
Sep 24, 2021·Frontiers in Genetics·Antonio ValcarcelJosé Díaz

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