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Nucleic Acids Research, 1985, Vol. 13, No. 19 6937-6953
© 1985

Articles

Human apolipoprotein B: identification of cDNA clones and characterization of mRNA

Margarete Mehrabian, Verne N. Schumaker, George C. Fareed1, Ruth West, David F. Johnson, Todd Kirchgessner, Hun-Chi Lin1, Xingbo Wang, Yuanhong Ma, Elizabeth Mendiaz1 and Aldons J. Lusis*

Departments of Medicine, Microbiology and Molecular Biology Institute UCLA, Los Angeles, CA 90024 1International Genetic Engineering, Inc. 1545 17th Street, Santa Monica, CA 90404, USA

*To whom correspondence should be addressed

Received July 15, 1985. Accepted September 9, 1985.

Apolipoprotein B (apoB) is a major protein component of low density and very low density lipoproteins. Because of its large size and heterogeneity, molecular studies of apoB have been difficult, and its structure and regulation remain poorly understood. We now report the identification of human apoB cDNA clones by antibody screening of hepatoma libraries in the expression vector {lambda}gtll. Both oligo(dT) primed and random primed libraries were constructed and screened with polyclonal antibodies to intact apeB, as well as with antibodies raised against a synthetic peptide based on the limited amino acid sequence available for apoB. The identity of the clones was unambiguously established by comparisons of the cloned cDNA sequences with apoB amino acid sequences. The clones hybridize to an exceptionally large 20 kb mRNA that is present in liver and intestine but not other tissues examined, consistent with the distribution expected from protein biosynthetic studies. The properties of the mRNA have implications for the biogenesis of the multiple apoB molecular weight forms secreted by liver and intestine.


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