scholarly journals Separation of the bovine colostrum M-1 glycoprotein into two components

1969 ◽  
Vol 115 (4) ◽  
pp. 817-822 ◽  
Author(s):  
Anatoly Bezkorovainy ◽  
Dietmar Grohlich
Keyword(s):  
Molecular Weight ◽  
Sialic Acid ◽  
Absorption Maximum ◽  
Periodate Oxidation ◽  
Bovine Colostrum ◽  
Carbohydrate Moiety ◽  
Elimination Reaction ◽  
Acid Glycoprotein ◽  
No Absorption

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 β-elimination reaction. 4. Periodate oxidation experiments showed that sialic acid was linked to galactose in both proteins.

scholarly journals Isolation and characterization of a glycoprotein from human colostrum

1973 ◽  
Vol 135 (4) ◽  
pp. 875-880 ◽  
Author(s):  
James H. Nichols ◽  
Anatoly Bezkorovainy
Keyword(s):  
Molecular Weight ◽  
Sialic Acid ◽  
Blood Group ◽  
Group Activity ◽  
Acid Glycoprotein ◽  
Isolation And Characterization ◽  
Human Colostrum ◽  
No Absorption

A glycoprotein was isolated from the M-1 acid glycoprotein fraction of human colostrum. It had a molecular weight of 31200 and contained 27% galactose, 21.7% hexosamine, 8.0% fucose and 10.8% sialic acid by weight. The glycoprotein had no absorption maxima in the 240–300nm region, and was virtually free of ABH(O) and M and N blood-group activity. Alkaline borohydride cleavage of the glycoprotein resulted predominantly in the destruction of threonine and galactosamine.

The carbohydrate portions of milk glycoproteins

1979 ◽  
Vol 46 (2) ◽  
pp. 187-191 ◽  
Author(s):  
Pierre Jollès
Keyword(s):  
Sialic Acid ◽  
Secondary Structure ◽  
Milk Protein ◽  
Neuraminic Acid ◽  
Bovine Colostrum ◽  
Carbohydrate Moiety ◽  
Cow’S Milk ◽  
Threonine Residue ◽  
Cow's Milk

SUMMARYk-Casein is the main glycoprotein of cow's milk. Its polysaccharide part is O-glycosidically linked to threonine residue 133. It contains only 3 different sugars (Gal, GalNAc, NeuNAc), but a microheterogeneity has been detected at the sugar level. Two main polysaccharides have so far been characterized. The structure of the trisaccharide is NeuNAc α → 3 Gal β1 →3 GalNAc; the tetrasaccharide contains one additional sialic acid. The polysaccharide part of ovine k-casein resembles that of bovine k-casein, but contains also N-glycolyl neuraminic acid. Human k-casein contains 3 times more carbohydrate than bovine k-casein with 2 additional sugars, GlcNAc and Fuc. The various polysaccharide parts isolated from bovine colostrum k-caseinoglycopeptide are much more complex than those obtained from the normal glycopeptide, indicating an evolution of the sugar part as a function of time after parturition. Some aspects of the secondary structure of k-casein and the role of the sugar part are discussed. The carbohydrate moiety of another milk protein, human lactotransferrin, is also discussed briefly. It is comprised of 2 identical glycan groups, N-glycosidically linked to the protein, and quite different from the k-casein carbohydrate moiety.

scholarly journals Carbohydrate PEGylation, an approach to improve pharmacological potency

2014 ◽  
Vol 10 ◽  
pp. 1433-1444 ◽  
Author(s):  
M Eugenia Giorgi ◽  
Rosalía Agusti ◽  
Rosa M de Lederkremer
Keyword(s):  
Molecular Weight ◽  
Polyethylene Glycol ◽  
Sialic Acid ◽  
Half Life ◽  
Viral Infections ◽  
Carbohydrate Moiety ◽  
Covalent Attachment ◽  
Low Molecular Weight ◽  
Pharmacokinetic Properties

Conjugation with polyethylene glycol (PEG), known as PEGylation, has been widely used to improve the bioavailability of proteins and low molecular weight drugs. The covalent conjugation of PEG to the carbohydrate moiety of a protein has been mainly used to enhance the pharmacokinetic properties of the attached protein while yielding a more defined product. Thus, glycoPEGylation was successfully applied to the introduction of a PEGylated sialic acid to a preexisting or enzymatically linked glycan in a protein. Carbohydrates are now recognized as playing an important role in host–pathogen interactions in protozoal, bacterial and viral infections and are consequently candidates for chemotherapy. The short in vivo half-life of low molecular weight glycans hampered their use but methods for the covalent attachment of PEG have been less exploited. In this review, information on the preparation and application of PEG-carbohydrates, in particular multiarm PEGylation, is presented.

scholarly journals Studies on the carbohydrate moiety of α1-acid glycoprotein (orosomucoid) by using alkaline hydrolysis and deamination by nitrous acid

1971 ◽  
Vol 124 (3) ◽  
pp. 591-604 ◽  
Author(s):  
M. Isemura ◽  
K. Schmid
Keyword(s):  
Sialic Acid ◽  
Acid Hydrolysis ◽  
Alkaline Hydrolysis ◽  
Nitrous Acid ◽  
Rapid Determination ◽  
Carbohydrate Moiety ◽  
Gas Liquid Chromatography ◽  
Acid Glycoprotein ◽  
Acetylneuraminic Acid ◽  
First Time

Alkaline hydrolysis followed by deamination with nitrous acid was applied for the first time to a glycoprotein, human plasma α1-acid glycoprotein (orosomucoid). This procedure, which specifically cleaves the glycosaminidic bonds, yielded well-defined oligosaccharides. The trisaccharides, which were obtained from the native protein, consisted of a sialic acid derivative, galactose and 2,5-anhydromannose. The linkage between galactose and 2,5-anhydromannose is most probably a (1→4)-glycosidic bond. A hitherto unknown linkage between N-acetylneuraminic acid and galactose was also established, namely a (2→2)-linkage. The three linkages between sialic acid and galactose described in this paper appear to be about equally resistant to mild acid hydrolysis. The disaccharide that was derived from the desialized glycoprotein consisted of galactose and 2,5-anhydromannose. Evidence was obtained for the presence of a new terminal sialyl→N-acetylglucosamine disaccharide accounting for approximately 1mol/mol of protein. The presence of this disaccharide may explain the relatively severe requirements for the complete acid hydrolysis of the sialyl residues. The present study indicates that alkaline hydrolysis followed by nitrous acid deamination in conjunction with gas–liquid chromatography will afford relatively rapid determination of the partial structure of the complex carbohydrate moiety of glycoproteins.

scholarly journals Gel filtration of sialoglycoproteins

1978 ◽  
Vol 173 (1) ◽  
pp. 315-319 ◽  
Author(s):  
J A Alhadeff
Keyword(s):  
Molecular Weight ◽  
Sialic Acid ◽  
Human Liver ◽  
Gel Filtration ◽  
Lower Molecular Weight ◽  
Acid Glycoprotein ◽  
Molecular Weights ◽  
Bovine Submaxillary Mucin

The role of sialic acid in the gel-filtration behaviour of sialoglycoproteins was investigated by using the separated isoenzymes of purified human liver alpha-L-fucosidase and several other well-known sialic acid-containing glycoproteins (fetuin, alpha1-acid glycoprotein, thyroglobulin and bovine submaxillary mucin). For each glycoprotein studied, gel filtration of its desialylated derivative gave an apparent molecular weights much less than that expected just from removal of sialic acid. For the lower-molecular-weight glycoproteins (fetuin and alpha1-acid glyocprotein), gel filtration of the sialylated molecules led to apparent molecular weights much larger than the known values. The data indicate that gel filtration cannot be used for accurately determining the molecular weights of at least some sialoglycoproteins.

Alternative Tanning Agent for Leather Industry from a Sustainable Source

2021 ◽  
Vol 116 (3) ◽  
Author(s):  
Cigdem Kilicarislan Ozkan ◽  
Hasan Ozgunay
Keyword(s):  
Molecular Weight ◽  
Corn Starch ◽  
Periodate Oxidation ◽  
Gel Permeation Chromatography ◽  
Proton Nuclear Magnetic Resonance ◽  
Resonance Spectroscopy ◽  
Leather Industry ◽  
Sodium Metaperiodate ◽  
Gel Permeation ◽  
Aldehyde Content

Dialdehyde starches with different aldehyde content from native corn starch were prepared by sodium periodate oxidation to be used as a tanning agent in leather making. For this purpose, native corn starch was oxidized with sodium metaperiodate in different molar ratios. After oxidation processes, the yields, solubility in water and aldehyde contents of the obtained dialdehyde starches were determined as well as structure characterizations by Proton Nuclear Magnetic Resonance Spectroscopy, Fourier Transform Infrared Spectroscopy and Gel Permeation Chromatography. Evaluating the gel permeation chromatography data, the dialdehyde starch samples which were thought to be in appropriate molecular weight/size to penetrate into skin fibers were selected to be used in the tanning process. Their tanning abilities were evaluated by investigating hydrothermal stabilities, filling and fiber isolation characteristics and physical properties determined by mechanical tests and organoleptically. From the evaluation of the results, it was revealed that sodium metaperiodate oxidized starches which have appropriate molecular weight and adequate aldehyde content has a remarkable tanning effect and can be utilized as a tanning agent with the advantages of not necessitating pickling process which means saving time and simplifying the production but more importantly offering an important advantage from an environmental point of view.

scholarly journals Effects of pronase and neuraminidase treatment on a myelin-associated glycoprotein in developing brain

1976 ◽  
Vol 156 (1) ◽  
pp. 143-150 ◽  
Author(s):  
R H Quarles
Keyword(s):  
Molecular Weight ◽  
Sialic Acid ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Weight Class ◽  
Developmental Difference ◽  
Adult Rats ◽  
Neuraminidase Treatment

Rats (14 days old) were injected with [14c]fucose and young adult rats with [3H]fucose in order to label the myelin-associated glycoproteins. As previously reported, the major [14C]fucose-labelled glycoprotein in the immature myelin had a higher apparent molecular weight on sodium dodecyl sulphate/polyacrylamide gels that the [3H]fucose-labelled glycoprotein in mature myelin. This predominant doubly labelled glycoprotein component was partially purified by preparative gel electrophoresis and converted to glycopeptides by extensive Pronase digestion. Gel filtration on Sephadex G-50 separated the glycopeptides into several clases, which were designted A,B, C AND D, from high to low molecular weight. The 14C-labelled glycopeptides from immature myeline were enriched in the highest-molecular-weight class A relative to the 3H-labelled glycopeptides from mature myelin. Neuraminidase treatment of the glycoprotein before Pronase digestion greatly decreased the proportion of glycopeptides fractionating in the higher-molecular-weight classes and largely eliminated the developmental differences that were apparent by gel filtration. However, neuraminidase treatment did not decrease the magnitude of the developmental difference revealed by electrophoresing the intact glycoprotein on sodium dodecyl sulphate gels, although it did decrease the apparent molecular weight of the glycoprotein from both the 15-day-old and adult rats by an amount comparable in magnitude to that developmental difference. The results from gel filtration of glycopeptides indicate that there is a higher content of large molecular weight, sialic acid-rich oligosaccharide units in the glycoprotein of immature myelin. However, the higher apparent molecular weight for the glycoprotein from 15-day-old rats on sodium dodcyl sulphate gels is not due primarily to its higher sialic acid content.

Porcine Sugar Nucleotide: Glycoprotein Glycosyltransferases. I. Blood Serum and Liver Sialyltransferase

1971 ◽  
Vol 49 (7) ◽  
pp. 829-837 ◽  
Author(s):  
Roger L. Hudgin ◽  
Harry Schachter
Keyword(s):  
Sialic Acid ◽  
High Speed ◽  
Liver Homogenate ◽  
Acetone Powder ◽  
Acid Glycoprotein ◽  
Acetylneuraminic Acid ◽  
Pork Liver ◽  
Terminal Galactose ◽  
And Function ◽  
Powder Extract

The properties of CMP-N acetylneuraminic acid: glycoprotein sialyltransferase have been studied in pork serum, a crude pork liver homogenate, and a soluble acetone powder extract prepared from pork liver. Whereas the crude liver homogenate enzyme is activated by the detergent Triton X-100, this detergent has no effect on the activities of either serum or acetone powder extract; since high-speed centrifugation does not sediment the enzyme activities of the latter two preparations, it is concluded that they are soluble. Comparison of the membrane-bound and soluble liver enzymes indicates that the membrane modifies kinetic behavior only to a limited extent. In both liver and serum, a single sialyltransferase is responsible for incorporation of sialic acid into α1-acid glycoprotein, fetuin, and N-acetyllactosamine, and sialic acid incorporation occurs whenever a terminal galactose linked (β, 1 → 4) to a penultimate N-acetylglucosamine is presented to the enzyme. Although the serum enzyme resembles the liver enzyme, both the source and function of serum sialyltransferase are unknown.

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