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At least 19 recordsLinked to original sources
PubMed1995

Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid.

A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 50 kDa. The substrate specificity of macluralisin towards synthetic peptides and insulin B-chain is similar to that of cucumisin, a subtilisin-like proteinase from melon fruit. The enzyme is completely inhibited by diisopropylfluorophosphate. Its amino-acid composition resembles that of a serine proteinase isolated from the Cucurbitaceae. The N-terminal sequence has 33% of its residues identical to those of the sequence of fungal subtilisin-like proteinase K. Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom.

Amino Acid Sequence↗
PubMed1985

Interaction of Salmonella telaviv with Maclura pomifera lectin.

Salmonella telaviv, Salmonella tranoroa, and Salmonella illinois were examined for their ability to interact with 15 purified lectins of known sugar specificity. The only interaction observed was between the lectin of Maclura pomifera and S. telaviv. M. pomifera lectin specifically agglutinated suspensions of S. telaviv and precipitated with its purified lipopolysaccharide and isolated lipid A free O polysaccharide. Quantitative inhibition assays showing methyl-alpha-D-galactopyranoside and N-acetyl-D-galactosamine to be potent inhibitors of Maclura lectin precipitation by S. telaviv O polysaccharide suggest that the interaction is mediated by D-galactose or N-acetyl-D-galactosamine units of bacterial polysaccharide structure, or both.

Agglutination↗
PubMed1991

Inhibitory action of extracts of Maclura aurantiaca and Epilobium hirsutum on tumour models in mice.

Primary screening of alcohol extracts of fruits of Maclura aurantiaca (Moraceae) and the overground part of Epilobium hirsutum (Onagraceae) was conducted in order to test the anti-tumour action on models in mice. Applied in doses of 100 mg/kg and 90 mg/kg, Maclura extract increased the life span of the mice by 158 and 152% accordingly in leucosis P-388 and ascitic tumour of Ehrich. In doses of 1 mg/kg and 3 mg/kg the Epilobium extract prolonged the life span of the mice by 156 and 158% accordingly in leucosis P-388 and ascitic tumour of Ehrlich.

Animals↗
PubMed2005

Novel methods to extract flavanones and xanthones from the root bark of Maclura pomifera.

A comparison between the extraction yields of xanthones and flavanones from the root bark of the Maclura pomifera by solid-liquid extraction (SLE), matrix solid phase dispersion (MSPD), and an alternative method using sea sand as a sample disruptor, is presented here. Two extraction solvents were used for all extraction techniques, dichloromethane and methanol:water, (9:1, v/v). The extraction procedures were reproducible as the R.S.D. values were less than 5% for almost all compounds. A recovery above 80% was obtained for macluraxanthone using the sea sand extraction procedure. Statistical treatment, ANOVA-single factor, was used to evaluate the different extraction procedures, and homogenization of plant material with sand followed by elution with dichloromethane provided the most efficient and rapid extraction method.

Chromatography, High Pressure Liquid↗
PubMed2006

Anti-inflammatory and antinociceptive potential of Maclura pomifera (Rafin.) Schneider fruit extracts and its major isoflavonoids, scandenone and auriculasin.

The aqueous, ethanolic and chloroform extracts and two prenylated isoflavones: scandenone (I) and auriculasin (II), isolated from the fruits of Maclura pomifera (Rafin.) Schneider, were investigated for their in vivo anti-inflammatory and antinociceptive activity. For the anti-inflammatory activity, both carrageenan-induced hind paw edema and 12-O-tetradecanoyl-13-acetate (TPA)-induced mouse ear edema models and for the antinociceptive activity, p-benzoquinone-induced abdominal constriction test were used. Scandenone, the chloroform and the ethanolic extracts were shown to possess antinociceptive activity and anti-inflammatory activity on carrageenan-induced hind paw edema model at 100 mg/kg dose. The same compound and the extract were also found to be highly active in (TPA)-induced mouse ear edema model whereas auriculasin and the H(2)O extract showed to be inactive in all of the assays.

Animals↗
PubMed2003

Antioxidant isoflavones in Osage orange, Maclura pomifera (Raf.) Schneid.

Recent findings that many human chronic diseases are associated with oxidative stresses have instigated the search for dietary antioxidants. Many phytochemicals, particularly phenolic compounds, have been found to possess strong antioxidant activity and reduce the risks of those diseases. Isoflavones, a special phenolic group found in soybean, have been found to act as antioxidants in some model systems. This study investigated the isoflavone content in a unique nonedible tree fruit, Osage orange [Maclura pomifera (Raf.) Schneid], and methods for the extraction, identification, and quantification of the two major isoflavones, osajin and pomiferin, were developed. The ethyl acetate extract contained 25.7% osajin and 36.2% pomiferin, and the two isoflavones were at 9.5 g kg(-1) of fresh Osage orange. Two model systems, FRAP and beta-CLAMS, were used to measure the antioxidant activity of these two isoflavones. Pomiferin was found to be a strong antioxidant in both systems, comparable to the antioxidant vitamins C and E and the synthetic antioxidant BHT. Osajin and the two soybean isoflavones (genistein and daidzein) showed no antioxidant activity. Although the Osage orange fruit is not a food source, it is considered to be safe and, therefore, a potentially good source of an antioxidant nutraceutical and functional food ingredient.

Acrolein↗
PubMed2003

Antioxidant chalcone glycosides and flavanones from Maclura (Chlorophora) tinctoria.

Four chalcone glycosides (1-4), including three new natural products, and three flavanones (5-7) were isolated from the methanol extract of stem bark of Maclura tinctoria. The new compounds have been characterized as 4'-O-beta-D-(2' '-p-coumaroyl)glucopyranosyl-4,2',3'-trihydroxychalcone (1), 4'-O-beta-D-(2' '-p-coumaroyl-6' '-acetyl)glucopyranosyl-4,2',3'-trihydroxychalcone (2), and 3'-(3-methyl-2-butenyl)-4'-O-beta-D-glucopyranosyl-4,2'-dihydroxychalcone (3); the known derivatives were elucidated as 4'-O-beta-D-(2' '-acetyl-6' '-cinnamoyl)glucopyranosyl-4,2',3'-trihydroxychalcone (4), eriodictyol 7-O-beta-D-glucopyranoside (5), naringenin (6), and naringenin 4'-O-beta-D-glucopyranoside (7). Their structures were determined by 1D and 2D NMR and ESIMS. The antioxidant activity of all the isolated compounds was determined by measuring free-radical-scavenging effects using two different assays, namely, the Trolox Equivalent Antioxidant Capacity (TEAC) assay and the coupled oxidation of beta-carotene and linoleic acid (autoxidation assay). The results showed that compound 3 was the most active in both antioxidant assays.

Antioxidants↗
PubMed2001

The yeast community of sap fluxes of Costa Rican Maclura (Chlorophora) tinctoria and description of two new yeast species, Candida galis and Candida ortonii.

We report on the yeast community associated with sap fluxes of Maclura tinctoria, family Moraceae, in the dry forest of the Area de Conservación Guanacaste, Costa Rica. Eleven samples yielded seven hitherto undescribed ascomycetous yeasts in the genera Candida and Myxozyma. We describe the two most abundant as new species. Candida galis utilizes very few carbon compounds limited to some alcohols and acids. Analysis of rDNA sequences suggests that it occupies a basal position with respect to the Pichia anomala clade, with no obvious sister species. Candida ortonii is also restricted in nutritional breadth, and growth is generally very slow. It is a sister species to Candida nemodendra. The type cultures are: C. galis, strain UWO(PS)00-159.2=CBS 8842; and C. ortonii, strain UWO(PS)00-159.3=CBS 8843.

Candida↗
PubMed1975

Isolation of 19alpha-H-lupeol from Maclura pomifera.

A reinvestigation of the constituents of the Osage orange (maclura pomifera) yielded, in addition to the previously reported triterpenses (lupeol, butyrospermol, and lupan-3beta,20-diol), the pigments osajin and pomiferin, and a previously unreported constituent. The structure of this new compound was investigated. On the basis of spectroscopic and chemical data, it appeared to be an epimer of lupeol and is referred to as 19alpha-H-lupeol.

Acetylation↗
PubMed1989

A histochemical localization on Maclura pomifera lectin during osteogenesis.

Mandibular condyles of 4-week-old Wistar strain rats and mandibles of ICR strain mice from 14 days gestation stage to 2 days postnatal stage were used to investigate the localization of Maclura pomifera lectin (MPA) during two modes of osteogenesis. During endochondral ossification of the mandibular condyle, MPA was only localized at the peripheral regions of calcified cartilage after the destruction of chondrocyte lacunae. Bone extracellular matrix (ECM) was not reacted with MPA. In intramembranous ossification of mice mandibles, MPA was stained intensively in the early bone ECM. The intensity of the MPA reaction decreased during bone development. In both cases of osteogenesis, chondroclasts and osteoclasts showed the strong affinity to MPA. These results indicated that the time- and position-specific changes within ECM proceeded during osteogenesis and that MPA was the useful probe to detect chondroclasts and osteoclasts.

Animals↗
PubMed1988

Ultrastructural demonstration of Maclura pomifera agglutinin binding sites in the membranocystic lesions of membranous lipodystrophy (Nasu-Hakola disease).

This paper reports three cases of membranous lipodystrophy (Nasu-Hakola disease) in two families and studies the carbohydrate components of membranocystic lesions in all three cases, using twelve kinds of lectins labelled by horseradish peroxidase (HRP). Maclura pomifera agglutinin (MPA), which specifically binds alpha-D-galactose residues, strongly stained typical membranocystic lesions, whereas the other lectins did not. However, Helix pomatia agglutinin (HPA), which specifically binds to N-acetyl-D-galactosamine (GalNAc), stained the membranes of degenerated adipose cells. These were thought to appear during the initial or early stage of the membranocystic lesions. This suggests that a change of carbohydrate residues occurs during the formation of the membranocystic lesions. We also investigated the lectin binding sites at the ultrastructural level using MPA-HRP colloidal gold (CG) conjugate. In the well developed membrane, CG particles were arranged regularly along the minute tubular structures. On the other hand, there were a few irregularly spaced CG particles on the thinner membranes and also on the membranes of the degenerating adipose cells. No CG particles labelled the cell membranes of normal adipose cells. The presence of alpha-D-galactose residues in the membranocystic lesions is demonstrated for the first time at the electron microscopic level.

Adipose Tissue↗
PubMed1982

Isolation of the Maclura pomifera hemagglutinin on a deoxymelibiotol affinity support and preliminary characterization by buffer electrofocusing and high-performance liquid chromatography.

Maclurin, the potent non-specific blood-group hemagglutinin present in extracts of Maclura pomifera, has been purified by a new biospecific affinity-chromatographic procedure. Additional studies have indicated that this hemagglutinin occurs as five closely related tetrameric protein isoforms derived from two non-covalently-linked polypeptide chains, mol. wts. ca. 10,000 and 13,000 respectively. Buffer electrofocusing fractionated the lectin into 12 components; the major isolectin exhibited an isoelectric point at pH 4.8.

Amino Acids↗
PubMed1991

Comparison of the Maclura pomifera lectin-binding glycoprotein in late fetal and adult rat lung.

The lectin, Maclura pomifera agglutinin (MPA), binds to alpha-galactose residues of glycoproteins on the apical surface of type II alveolar cells. It has recently been shown to bind to macrophages. We isolated the cell surface glycoprotein, which binds the MPA lectin, from fetal and adult rat whole lung to determine if changes in this glycoprotein occur during development from fetal to adult life. The glycoprotein was purified from whole lung cell membranes by lectin affinity chromatography that resulted in 10(5)-fold enrichment. The MPA binding glycoproteins from both fetal and adult lung had the same apparent molecular weight of 170 kD as determined by sodium dodecylsulfate-polyacrylamide gel electrophoresis. Amino acid analysis revealed similar composition of the fetal and adult proteins. Two-dimensional peptide maps of the 170 kD proteins isolated from fetal and adult lung were also similar. These data indicate that the glycoprotein that binds MPA to lung cell membranes does not change during this stage of development. Our method for the isolation of this glycoprotein can be used for the generation of antibodies or other molecular probes for further study of this protein.

Amino Acids↗
PubMed2005

Polyvalent GalNAcalpha1-->Ser/Thr (Tn) and Galbeta1-->3GalNAcalpha1-->Ser/Thr (T alpha) as the most potent recognition factors involved in Maclura pomifera agglutinin-glycan interactions.

The agglutinin isolated from the seeds of Maclura pomifera (MPA) recognizes a mucin-type disaccharide sequence, Galbeta1-->3GalNAc (T) on a human erythrocyte membrane. We have utilized the enzyme-linked lectinosorbent assay (ELLSA) and inhibition assay to more systematically analyze the carbohydrate specificity of MPA with glyco-recognition factors and mammalian Gal/GalNAc structural units in lectin-glycoform interactions. From the results, it is concluded that the high densities of polyvalent GalNAcalpha1-->Ser/Thr (Tn) and Galbeta1-->3GalNAcalpha1-->Ser/Thr (T(alpha)) glycotopes in macromolecules are the most critical factors for MPA binding, being on a nanogram basis 2.0 x 10(5), 4.6 x 10(4) and 3.9 x 10(4) more active than monovalent Gal, monomeric T and Tn glycotope, respectively. Other carbohydrate structural units in mammalian glycoconjugates, such as human blood group Sd (a+) related disaccharide (GalNAcbeta1-->4Gal) and Pk/P1 active disaccharide (Galalpha1-->4Gal) were inactive. These results demonstrate that the configurations of carbon-4 and carbon-2 are essential for MPA binding and establish the importance of affinity enhancement by high-density polyvalencies of Tn/T glycotopes in MPA-glycan interactions. The overall binding profile of MPA can be defined in decreasing order as high density of polyvalent Tn/T(alpha) (M.W. > 4.0 x 10(4)) >> Tn-containing glycopeptides (M.W. < 3.0 x 10(3)) > monomeric T/Tn and P (GalNAcbeta1-->3Gal) > GalNAc > Gal >> Man, L: ARA: , D: Fuc and Glc (inactive). Our findings should aid in the selection of this lectin for elucidating functions of carbohydrate chains in life processes and for applications in the biomedical sciences.

Animals↗
PubMed1989

Homology of the D-galactose-specific lectins from Artocarpus integrifolia and Maclura pomifera and the role of an unusual small polypeptide subunit.

The Maclura pomifera agglutinin (MPA) was purified by affinity chromatography from a seed extract and its properties were compared with those of the Artocarpus integrifolia lectin, jacalin. Reverse-phase high-performance liquid chromatography showed both proteins had multiple forms of a small approximately 20-residue polypeptide chain in addition to the major 12,000 Mr subunit. The amino acid sequences of the small chains and the N-terminal sequences of the large subunits showed considerable similarity between the two proteins, approximately 60% identical residues. The homology of the proteins was confirmed by the similarity of their circular dichroism and fluorescence emission spectra. MPA showed much greater spectral changes upon binding methyl alpha-D-galactoside, suggesting it has complete activity rather than the partial activity found for jacalin. The binding of methyl alpha-D-galactoside by MPA was measured by fluorescence titration; the KA was 1.9 X 10(4) M-1 compared to 3.4 X 10(4) M-1 for jacalin. MPA also precipitated human IgA1 in the same manner as jacalin. The spectra indicate the involvement of tryptophan and tyrosine residues in the binding site of these lectins. Since a tryptophan residue is conserved in all the small subunits, they may form part of the binding site.

Amino Acid Sequence↗
PubMed1991

The amino acid sequences of jacalin and the Maclura pomifera agglutinin.

Amino acid sequences for the alpha-chains of the Moraceae lectins, jacalin and Maclura pomifera agglutinin, were determined by protein sequencing. Both are 133 residues long and contain several genetically variant positions; the overall homology is 85%. A possible site for the known glycopeptide of jacalin was located. The alpha-chains have a conserved tryptophan residue that may be part of the binding-site.

Amino Acid Sequence↗
PubMed1989

Crystallization and preliminary X-ray diffraction studies of the complex of Maclura pomifera agglutinin with the disaccharide Gal beta 1-3GalNAc.

Single crystals of Maclura pomifera agglutinin, a seed lectin from the Moraceae family, complexed with the disaccharide Gal beta 1-3GalNAc have been obtained by the method of vapor diffusion with Li2SO4 as precipitant at pH 4.5. The crystals belong to the trigonal space group P3(1)21 or P3(2)21, with a = b = 67.4 A, c = 149.3 A. They contain two subunits per asymmetric unit and diffract beyond 2.7 A. This and other evidence indicate that both this lectin and the Artocarpus integrifolia lectin, jacalin, have dimeric structures rather than the tetrameric structures previously proposed.

Antigens, Surface↗
PubMed1988

Identification and characterization of the pulmonary alveolar type II cell Maclura pomifera agglutinin-binding membrane glycoprotein.

The lectin Maclura pomifera agglutinin (MPA) binds to the apical surface of pulmonary alveolar type II but not type I cells. We show that MPA binds to a single membrane glycoprotein in type II cells with a molecular mass of 230 kDa in the rabbit and 200 kDa in the rat. The glycoprotein has an abundance of terminal N-acetylgalactosamine residues. It is a hydrophilic integral membrane protein suggesting that it has an extensive extramembrane domain or is an ion channel. The glycoprotein is similar in rat and rabbit, with the exception that the rat glycoprotein is partially sialylated and is trypsin sensitive. The MPA-binding glycoprotein represents a new integral membrane marker of the apical domain of the pulmonary alveolar type II cell.

Animals↗