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 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 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.

Isolation and Characterization of Plasminogen Activator from Pig Leucocytes

1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Ph Optimum ◽  
Isolation And Characterization ◽  
Ph Range ◽  
Inhibition Studies ◽  
Final Purification

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.

Preparation and Characterization of the High Molecular Weight [3H]Hyaluronic Acid

1992 ◽  
Vol 57 (10) ◽  
pp. 2151-2156 ◽  
Author(s):  
Peter Chabreček ◽  
Ladislav Šoltés ◽  
Hynek Hradec ◽  
Jiří Filip ◽  
Eduard Orviský
Keyword(s):  
Molecular Weight ◽  
Hyaluronic Acid ◽  
High Molecular Weight ◽  
Methyl Bromide ◽  
High Performance ◽  
Hydrogen Atoms ◽  
Isolation And Characterization ◽  
Labelling Procedure ◽  
Enzymatic Depolymerization

Two methods for the preparation of high molecular weight [3H]hyaluronic acid were investigated. In the first one, hydrogen atoms in the molecule were replaced by tritium. This isotopic substitution was performed in aqueous solution using Pd/CaCO3 as the catalyst. In the second method, the high molecular weight hyaluronic acid was alkylated with [3H]methyl bromide in liquid ammonia at a temperature of -33.5 °C. High-performance gel permeation chromatographic separation method was used for the isolation and characterization of the high molecular weight [3H]hyaluronic acid. Molecular weight parameters for the labelled biopolymers were Mw = 128 kDa, Mw/Mn = 1.88 (first method) and Mw = 268 kDa, Mw/Mn = 1.55 (second method). The high molecular weight [3H]hyaluronic acid having Mw = 268 kDa was degraded further by specific hyaluronidase. Products of the enzymatic depolymerization were observed to be identical for both, labelled and cold biopolymer. This finding indicates that the described labelling procedure using [3H]methyl bromide does not induce any major structural rearrangements in the molecule.

scholarly journals Isolation and characterization of novel glycolipids with blood group A-related structures: galactosyl-A and sialosylgalactosyl-A.

1987 ◽  
Vol 262 (29) ◽  
pp. 14228-14234
Author(s):  
H Clausen ◽  
S B Levery ◽  
E D Nudelman ◽  
M Stroud ◽  
M E Salyan ◽  
...  
Keyword(s):  
Blood Group ◽  
Blood Group A ◽  
Isolation And Characterization ◽  
Group A
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