Some studies on the composition of bovine cortical-bone sialoprotein

Andrews, Anthony T.; Herring, G. M.; Kent, P. W.

doi:10.1042/bj1040705

Cited by 71 publications

(24 citation statements)

References 41 publications

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“…Qualitative identification of the hexosamines in the residues was by paper chromatography (Andrews et al, 1967) and was confirmed by data from the amino acid analyser. Quantitative assay of hexosamines was carried out by a modified Elson-Morgan procedure (Boas, 1953).…”

Section: Other Analytical Methodsmentioning

confidence: 99%

“…Total neutral 1974 NAVY-BEAN LECTIN monosaccharide was determined with mannose as standard by a modified anthrone procedure (Andrews et al, 1967) and confirmed by the orcinol method (Franr,ois et al, 1962).…”

Section: Other Analytical Methodsmentioning

confidence: 99%

“…These solutions were desalted and freed of amino acids by passage in distilled water through a short column (0.8 cm x 5.0 cm) of Dowex 1 (X 8; OHform), then through a similar column of Dowex 50 W (X 8: H+ form) and evaporated to dryness over NaOH pellets. The neutral monosaccharide residues were examined by paper chromatography as described previously (Andrews et al, 1967).…”

Section: Other Analytical Methodsmentioning

confidence: 99%

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Navy (haricot)-bean (Phaseolus vulgaris) lectin. Isolation and characterization of two components from a toxic agglutinating extract

Andrews¹

1974

Biochemical Journal

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Two protein components were isolated in a highly purified state from a toxic fraction from the navy (haricot) bean (Phaseolus vulgaris). One, a lectin, strongly agglutinated horse erythrocytes and leucocytes, agglutination being readily observable with both types of cell at a lectin concentration of 4mug/ml. The other component (component 1), although possessing some similarity in composition, was thought to be non-agglutinating or, at most, only very weakly so. Component 1 had a mol.wt. of about 143000 and a subunit mol.wt. of about 37000, suggesting a tetrameric structure probably with identical subunits. Alanine was the only N-terminal amino acid identified and the molecule was notable in being devoid of tryptophan and cysteine, low in methionine and high in leucine, glutamic acid and aspartic acid. The lectin was somewhat smaller (mol.wt. about 114000) and apparently also composed of four identical subunits of mol.wt. about 30000. Dansylation showed that arginine occupied the N-terminus of the polypeptide chain. Aspartic acid, serine, threonine and leucine were the predominant amino acids of the lectin, and the sulphur-containing amino acids were entirely absent. Both constituents were glycoproteins and the compositions of the carbohydrate portions (4.9% for component 1 and 8.1% for the lectin) were generally similar, consisting of mannose and glucosamine with smaller amounts of glucose and traces of xylose and arabinose.

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Section: Other Analytical Methodsmentioning

confidence: 99%

Section: Other Analytical Methodsmentioning

confidence: 99%

Section: Other Analytical Methodsmentioning

confidence: 99%

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Navy (haricot)-bean (Phaseolus vulgaris) lectin. Isolation and characterization of two components from a toxic agglutinating extract

Andrews¹

1974

Biochemical Journal

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“…One of these glycoproteins, alpha 2HS-glycoprotein, is derived from blood plasma and becomes incorporated into bone matrix during its formation [13,[15][16][17]. Another identified as a very acidic sialoprotein [18][19][20][21] is probably not blood borne and is particularly enriched in bone matrix [22]. Both have been reported to contain fucose residues, whereas collagen does not contain fucose [23].…”

Section: Discussionmentioning

confidence: 98%

Radioautographic visualization of3H-fucose incorporation into glycoprotein by osteoblasts and its deposition into bone matrix

Weinstock

1979

Calcif Tissue Int

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Summary. The elaboration of bone matrix glycoprotein by osteoblasts of alveolar bone was investigated by radioautography after the intravenous injection of 3H-fucose into young rats. At selected times after injection, animals were sacrificed by intracardiac perfusion and demineralized specimens were prepared for light and electron microscope radioautography.At 5 and 10 min after injection, when the blood fucose level was high, silver grains were restricted to the spheroidal and cylindrical saccules of the Golgi apparatus. At 20 min membrane-limited secretory granules were also labeled. By 35 min, the blood fucose level had dropped and silver grains were detected over the apical cortical cytoplasm, in association with secretory granules located therein. Some grains were present over osteoblast processes and the adjacent prebone matrix. By 4 h most of the silver grains had left the cell. At that time they were observed over prebone, adjacent to osteoblast processes, as well as over the prebone-bone junction where a distinct band of label was noted. In demineralized preparations an electron-dense granular material was present at the prebone-bone junction in association with collagen fibrils.These findings provide evidence that osteoblasts in alveolar bone synthesize fucose-containing glycoprotein and indicate that the addition of 3H-fucose occurs in the Golgi apparatus. The glycoprotein passes to the apical cortical cytoplasm by way of membrane-limited secretory granules, is exteriorized, and accumulates at the site where prebone transforms into bone (the prebone-bone junction). Since this is also the site of the calcification front, the deposition of labeled glycoprotein may be related to the deposition of bone mineral.Send offprint requests to M. Weinstock at the above address,

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“…I n order to determine the role of sialic acid in metal binding, sialic acid was removed from bone sialoprotein and the chondroitin sulphate-protein complex by mild hydrolysis in 0.1 N sulphuric acid a t 80" for 1 h [11,17].…”

Section: Methodsmentioning

confidence: 99%

The Binding of Americium and Plutonium to Bone Glycoproteins

Chipperfield

Taylor

1970

European Journal of Biochemistry

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By means of a gel filtration technique it is shown that plutonium and americium differ in their mode of binding to two glycoproteins isolated from bovine cortical bone. Plutonium binds more strongly than americium, plutonium binding is maximal a t pH 6 and americium a t p H 8, and sialic acid is involved in the binding of plutonium but not americium. The mechanisms by which these elements bind to glycoproteins in vitro are discussed.A number of metals are now known to concentrate in bone where they may cause serious pathological disturbances, including neoplasia. Some metals, for example strontium and radium, are associated with the hydroxyapatite of the mineral phase, but others, such as yttrium or the radioelements of the transuranic group, deposit predominantly in resting and resorbing areas on the endosteal and, to a lesser extent, periosteal surfaces of bone [I]. More information of the mechanisms of deposition of metals in bone would help to increase our understanding of both the general biochemistry of bone and of the induction of bone cancer and other pathological conditions by radioactive or non-radioactive metals deposited in bone.Observations of the deposition of yttrium, plutonium and americium in bone suggested that these elements might be bound by mucosubstances present at the bone surfaces [2,3]. The glycoproteins of bovine cortical bone have been studied extensively by Herring [a] and the binding of heavy metals to some of these substances has been demonstrated by other workers [5,6].So far two glycoprotein components of bovine bone have been described in detail [7]. The first is bone sialoprotein, a glycoprotein of molecular weight 25000 f 500 containing 40°/,, by weight of carbohydrate [8,9]: it is unusual in its high content of sialic, aspartic and glutamic acids [9]. The second is the bone chondroitin sulphate-protein complex [ 101 or, more correctly, the three chondroitin sulphateprotein complexes. The compositions of these three complexes are consistent with their being either free chondroitin sulphate or one or two chondroitin sulphate chains attached to a protein core whose properties appear t o be similar to those of bone sialoprotein [lo]. There are also other glycoproteins in bovine cortical bone The study of the binding of heavy metals to proteins is complicated by the pronounced tendency of such metals to hydrolyse a t neutral pH. Consequently it is not easy to use conventional methods for the study of reactions between proteins and heavy metals. This report describes the application of a previously published gel filtration procedure [ll] to the study of the mechanisms of binding of americium to bone sialoprotein and of plutonium and americium to the chondroitin sulphate-protein complex of bovine cortical bone. MATERIALS AND METHODS MaterialsBone sialoprotein and the chondroitin sulphateprotein complex, i.e. the mixture of the three complexes as normally prepared, were isolated from bovine cortical bone by methods based on those of Herring [4]. The later stages of these preparati...

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Some studies on the composition of bovine cortical-bone sialoprotein

Cited by 71 publications

References 41 publications

Navy (haricot)-bean (Phaseolus vulgaris) lectin. Isolation and characterization of two components from a toxic agglutinating extract

Navy (haricot)-bean (Phaseolus vulgaris) lectin. Isolation and characterization of two components from a toxic agglutinating extract

Radioautographic visualization of3H-fucose incorporation into glycoprotein by osteoblasts and its deposition into bone matrix

The Binding of Americium and Plutonium to Bone Glycoproteins

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