Some immunochemical properties of succinylated human transferrin and related proteins.
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Biomedical subjects
Publications and source records attributed to A Bezkorovainy.
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1. Two glycoproteins were isolated from the M-1 acid glycoprotein fraction of bovine colostrum. 2. The lighter glycoprotein had a molecular weight of 7200, contained about 28.4% of carbohydrate, and had an absorption maximum at 275nm. The heavier glycoprotein had a molecular weight of 12000, contained 39.0% of carbohydrate, and had no absorption maxima in the 240-300nm. range of the spectrum. 3. The carbohydrate moiety of both glycoproteins was removable from the polypeptide moiety under the conditions of the beta-elimination reaction. 4. Periodate oxidation experiments showed that sialic acid was linked to galactose in both proteins.
1. Apparently all disulphide bridges of transferrin and conalbumin were broken by reduction-alkylation, whereas sulphitolysis resulted in incomplete cleavage of disulphide bonds. 2. The molecular weights of reduced-alkylated and sulphitolysed transferrin and reduced-alkylated conalbumin were identical with those of native proteins in a number of solvents, indicating that these proteins exist as single polypeptide chains. 3. Viscosity studies indicated that reduced-alkylated transferrin possesses a partially ordered structure in 0-4m-urea, assumes a random-coil configuration in 6m-urea with a molecular weight of 84000 and is partially aggregated in 8m-urea.
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Initial rates of ferrous iron transport into Bifidobacterium bifidum var. pennsylvanicus were measured at low and high iron concentrations. The low affinity system (LAFIUS) had an apparent Km of 167 microM, the high affinity system (HAFIUS) had a Km of 50 microM. Iron removal from preloaded bifidobacteria revealed the existence of a labile and an inert iron pool in the bacterial cells. Iron uptake by the bifidobacteria was associated with lactate production, though lactate production could continue without iron uptake. Cessation of iron uptake and lactate production was not because of an exhaustion of any nutrient nor the accumulation of fermentation end products in the medium. It was apparently the result of an inactivation of the cellular enzyme machinery without replacing it through normal biosynthetic processes.
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