Isolation and characterization of a glycosphingolipid having a new sialic acid

Biochemistry ◽  
1969 ◽  
Vol 8 (12) ◽  
pp. 5082-5088 ◽  
Author(s):  
Senitiroh Hakomori ◽  
Terunobu Saito
Keyword(s):  
Sialic Acid ◽  
Isolation And Characterization

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.

scholarly journals Studies on gastric mucoproteins. The isolation and characterization of the mucoprotein of the water-soluble mucus from pig cardiac gastric mucosa

1971 ◽  
Vol 123 (5) ◽  
pp. 845-853 ◽  
Author(s):  
D. Snary ◽  
A. Allen
Keyword(s):  
Sialic Acid ◽  
Gastric Mucosa ◽  
Gel Filtration ◽  
Water Soluble ◽  
Group Activities ◽  
Isolation And Characterization ◽  
Two Peaks ◽  
Sepharose 4B

1. Gel filtration of the water-soluble radioactive mucus produced three radioactive fractions, fraction A excluded on Sepharose 4B, fraction B included on Sepharose 4B but excluded on Sephadex G-200, and fraction C included on Sephadex G-200. 2. The specific radioactivities of fractions A and B were the same, with fraction C a little lower, whether the material was labelled with 14C-labelled carbohydrate or with 3H-labelled protein prepared by incubation of mucosal scrapings in vitro with [U-14C]glucose or [G-3H]threonine respectively. 3. Fractions A and B had an analysis of protein 22%, hexose 28%, hexosamine 28%, fucose 10% and sialic acid 1%; fraction C had an analysis closely similar to this, except that it contained about 10% of a protein contaminant. 4. All three fractions had closely similar A and H blood-group activities. 5. Ultracentrifuge studies showed fractions A, B and C were polydisperse with s025,w values of 18.7S, 4.9S and 3.9S respectively. 6. The unfractionated water-soluble mucus contained only two peaks, fraction A 18.7S and a peak of 4.4S, which was a combination of fractions B and C. 7. The radioactive mucoprotein accounted for 85% by weight of the soluble mucus and the results show that it consisted of two distinct fractions A and B–C, which were chemically, biosynthetically and immunologically very similar.

scholarly journals The isolation and characterization of a glycoprotein from human thoracic aorta

1968 ◽  
Vol 109 (5) ◽  
pp. 883-896 ◽  
Author(s):  
M. J. Barnes ◽  
S. M. Partridge
Keyword(s):  
Molecular Weight ◽  
Sialic Acid ◽  
Proteolytic Activity ◽  
Thoracic Aorta ◽  
Deae Cellulose ◽  
Human Aorta ◽  
Isolation And Characterization ◽  
Intimate Association ◽  
Carbohydrate Digestion

1. A glycoprotein extracted by cold alkali from the walls of human aorta was purified by chromatography on DEAE-cellulose. 2. The compound was electrophoretically homogeneous and essentially so by chromatography on DEAE-cellulose. Ultracentrifugal examination revealed two components, and it is suggested that the faster-sedimenting component represents an aggregated form of the glycoprotein. 3. Glycoprotein preparations contained approx. 8% of carbohydrate. Digestion with Pronase yielded a glycopeptide fraction containing all the carbohydrate of the glycoprotein. The glycopeptide, of molecular weight about 7800, contained sialic acid, galactose, mannose, fucose and hexosamine in the approximate molar proportions 5:10:5:2:11. Sialic acid was terminal with respect to the polysaccharide chains. 4. Both elastase and elastomucoproteinases exhibited proteolytic activity towards the glycoprotein. Studies by other investigators have led to the conclusion that elastomucoproteinases attack protein–carbohydrate complexes occurring in intimate association with elastin in aorta and other tissues, and it is suggested that the glycoprotein may be identified with one of these compounds.

The isolation and characterization of 18 equine microsatellite loci, TKY272–TKY289

2000 ◽  
Vol 31 (2) ◽  
pp. 149-149 ◽  
Author(s):  
T Tozaki ◽  
H Kakoi ◽  
S Mashima ◽  
K Hirota ◽  
T Hasegawa ◽  
...  
Keyword(s):  
Microsatellite Loci ◽  
Isolation And Characterization
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