Anthraquinones (9,10-dioxoanthracenes) constitute an important class of natural and synthetic compounds with a wide range of applications. Besides their utilization as colorants, anthraquinone derivatives have been used since centuries for medical applications, for example, as laxatives and antimicrobial and antiinflammatory agents. Current therapeutic indications include constipation, arthritis, multiple sclerosis, and cancer. Moreover, biologically active anthraquinones derived from Reactive Blue 2 have been utilized as valuable tool compounds for biochemical and pharmacological studies. They may serve as lead structures for the development of future drugs. However, the presence of the quinone moiety in the structure of anthraquinones raises safety concerns, and anthraquinone laxatives have therefore been under critical reassessment. This review article provides an overview of the chemistry, biology, and toxicology of anthraquinones focusing on their application as drugs.

Anthraquinones As Pharmacological Tools and Drugs

The low molecular weight folate binding protein (FABP) has been purified 1000-fold to a specific activity of 7.2 gamma g of pteroylglutamic acid (PGA) bound per mg of protein. This purified FABP represents two protein bands that bind PGA on polyacrylamide disc gel electrophoreis, elutes from DEAE-cellulose in 0.001 M phosphate buffer, stains positive with PAS, Elutes from concanavalin A Sepharose affinity columns with methyl alpha-mannoside, and shows three major peaks (pl =6.8, 7.5, 8.2) by isotric focusing. The binding of PGA to purified FABP dependent on pH and is inhibited by urea...

The purification and characterization of the low molecular weight human folate binding protein using affinity chromatography.

The unsaturated vitamin B12 binding capacity of whole serum (UBBC) and of the three transcobalamins (TC) has been studied in patients with various haematological diseases including myeloproliferative disorders (MPD) and acute leukaemia. The binding capacity of TC I and TC III was increased in MPD; TC I being particularly high in chronic granulocytic leukaemia (CGL) and TC III especially raised in polycythaemia rubra vera (PRV) and in infectious leucocytosis. The binding capacity of both TC I and TC III correlated with blood neutrophil count and the ratio TC III/TC I was low in CGL and increased in PRV. TC II was increased in acute myelogenous leukaemia, during remission and blast cell crisis of CGL and in refractory anaemia with excess of myeloblasts but not in acute lymphoblastic leukaemia (ALL). TC II correlated inversely with blood neutrophil count. There is an inverse ratio between TC II and TC I at least in myelogenous leukaemia. These abnormalities are discussed in relation to granulocyte kinetics. TC III and TC I reflect probably the total body granulocyte pool and share some biochemical and immunological properties supporting the view that they have a common origin in the more mature stages of the granulocyte cell line while TC II probably originates partly in more primitive granulocytes.

The Three Transcobalamins in Myeloproliferative Disorders and Acute Leukaemia

Extraordinary elevations of serum vitamin B12 content and serum levels of vitamin B12 binding protein were found in three young patients with hepatoma. All had normal white-cell counts and no evidence of megaloblastosis. Despite a superficial resemblance to the alterations of vitamin B12 and vitamin B12 binders observed in chronic myeloid leukemia, the vitamin B12 binding protein in hepatoma serum exhibited distinct and unique properties that suggest a novel, tumor-related protein. (N Engl J Med 289:1053–1056, 1973)

A tumor-related vitamin B12 binding protein in adolescent hepatoma.

1. Serum from normal subjects has been chromatographed on Sephadex G-200 columns and the fractions containing transcobalamins 0, I and II have been identified. 2. The fractions corresponding to transcobalamin I contained, on average, 90% of the endogenous vitamin B12. Only 3% was attached to transcobalamin 0, and 7% was bound to transcobalamin II.

The Transport of Endogenous Vitamin B12 in Normal Human Serum

The vitamin B12-binding proteins in sera and leukocytes of healthy subjects and patients with chronic myelogenous leukemia (CML) were separated and partially purified by column chromatography as their cyanocobalamin complexes. The molecular weight of transcobalamin I and leukocyte B12-binding protein was 119,000, and that of transcobalamin II was 32,000 as determined by gel filtration. The electrophoretic mobilities were α1 for transcobalamin I, α2 for the leukocyte B12-binding protein, and α2-β for transcobalamin II. After treatment with neuraminidase or chromatographic purification, the mobilities of both transcobalamin I and the leukocyte B12-binding protein became β. Transcobalamin I and the leukocyte B12-binding protein gave a reaction of immunologic identity in immunodiffusion. The fact that leukocytes can produce B12-binding protein in vitro and the similarities between leukocyte B12-binding protein and transcobalamin 1 strongly suggest that CML transcobalamin I is derived from leukocytes.

Vitamin B12-binding Proteins in Normal and Leukemic Human Leukocytes and Sera

Publisher Summary This chapter describes the immunological and biochemical characterization of the low density lipoprotein (LDL) proteins. The lipoproteins of the human serum contain some genetic variants similar to those found in the gamma-globulins. The Lp(a) antigen was found in the LDL entities, characterized by a density of from 1050 to 1125 g/ml. This LDL fraction migrates in the zone electrophoresis in the alpha 2 - and beta-globulin area. It shows precipitation with anti-beta- and anti-alpha2-lipoprotein. The LDL can be separated from the high density lipoproteins and the other serum proteins by column chromatography on hydroxyapatite at a pH of 6.8 and a phosphate buffer molarity of 0.65. In the zone electrophoresis the apoprotein which is not dialyzable migrates to the albumin position. The total LDL and their subfractions at pH 6.8 differ in their peptide content, which is higher in the Lp(a +) fractions than in the Lp(a−) fractions. It is found that besides the first LDL fraction, which has a triglyceride content of about 30-40%, the triglyceride content of the other fractions is lower

Molecular Variation in an Intra- and Extracellular R-type Vitamin B12-binding Protein

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Vitamin B12-binding Proteins in Normal and Leukemic Human Leukocytes and Sera

Molecular Variation in an Intra- and Extracellular R-type Vitamin B12-binding Protein