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Cloning and expression of human apolipoprotein D cDNA.

Journal of Biological ChemistryPublished 1 December 1986Open access
Dennis Drayna, Ceri A. Fielding, J W McLean, B W Baer, G.R. Castro, Ella Chen
Citations220
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR

The amino acid sequence of human apolipoprotein D, a component of high density lipoprotein, has been obtained from the cloned cDNA sequence and has a high degree of homology to plasma retinol-binding protein and other members of the alpha 2u-globulin protein superfamily.

Abstract

The amino acid sequence of human apolipoprotein D, a component of high density lipoprotein, has been obtained from the cloned cDNA sequence. The 169-amino acid protein has no marked similarity to other apolipoprotein sequences, but has a high degree of homology to plasma retinol-binding protein and other members of the alpha 2u-globulin protein superfamily. Apolipoprotein D mRNA has been detected in human liver, intestine, pancreas, kidney, placenta, adrenal, spleen, and fetal brain tissue. Tissue culture cells transfected with the cloned cDNA secrete material that reacts with anti-apoD antibodies.

Keywords

MedicineBiochemistry, Genetics and Molecular Biology