A protein of 70000 molecular weight is joined by disulphide bridges to pig gastric-mucus glycoprotein

1980 ◽  
Vol 8 (3) ◽  
pp. 388-389 ◽  
Author(s):  
JEFFREY P. PEARSON ◽  
ADRIAN ALLEN
Keyword(s):  
Molecular Weight ◽  
Gastric Mucus ◽  
Mucus Glycoprotein

scholarly journals Polymeric structure of pig small-intestinal mucus glycoprotein. Dissociation by proteolysis or by reduction of disulphide bridges

1981 ◽  
Vol 195 (1) ◽  
pp. 277-285 ◽  
Author(s):  
M Mantle ◽  
D Mantle ◽  
A Allen
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Protein Molecule ◽  
Amino Acid Residues ◽  
Proteolytic Digestion ◽  
Gastric Mucus ◽  
Polymeric Structure ◽  
Mucus Glycoprotein ◽  
Intestinal Mucus ◽  
Small Intestinal

Pig small-intestinal mucus glycoprotein, of molecular weight 1.72 X 10(6), is cleaved by Pronase digestion into glycoprotein subunits of molecular weight 4.5 X 10(5). Of the protein component of the native glycoprotein 29% by weight was lost on Pronase digestion, with no loss of carbohydrate. The non-glycosylated region of the protein that was lost with proteolytic digestion had a broad spectrum of amino acid residues, in contrast with the glycosylated region of the protein, which was resistant to proteolysis and was rich in serine, threonine and proline residues. Reduction with 0.2M-mercaptoethanol dissociated the Pronase-digested glycoprotein subunits into smaller glycoprotein subunits of molecular weight 2.7 X 10(5). On reduction, the native glycoprotein was dissociated into subunits of molecular weight 2.4 X 10(5), a similar size to those obtained from reduction of the Pronase-digested glycoprotein. On reductive dissociation of the native glycoprotein, in addition to glycoprotein subunits, protein was also released principally as a component of 90000 molecular weight. This protein was separated quantitatively from the reduced glycoprotein in amounts compatible with one 90000-mol.wt. protein molecule per 1.72 X 10(6)-mol.wt. native glycoprotein molecule. No 90000-mol.wt. protein was released on reduction of the isolated Pronase-digested glycoprotein. Pig small-intestinal mucus glycoprotein is therefore a covalent polymer of glycoprotein subunits joined by disulphide bridges. This polymeric structure differs in important respects from that previously shown for gastric mucus, in particular with respect to the size and number of component subunits per native molecule.

scholarly journals Biosynthesis of Gastric Mucus Glycoprotein of the Rat

1989 ◽  
Vol 264 (18) ◽  
pp. 10431-10437
Author(s):  
J Dekker ◽  
W M O Van Beurden-Lamers ◽  
G J Strous
Keyword(s):  
Gastric Mucus ◽  
Mucus Glycoprotein

Two Types of Rat Gastric Mucus Glycoprotein Subunits1

1988 ◽  
Vol 103 (6) ◽  
pp. 1050-1053 ◽  
Author(s):  
Susumu Ohara ◽  
Kazuhiko Ishihara ◽  
Kyoko Hotta
Keyword(s):  
Gastric Mucus ◽  
Mucus Glycoprotein

N-Terminal amino acids of purified pig gastric mucus glycoprotein

1983 ◽  
Vol 11 (6) ◽  
pp. 765-766
Author(s):  
ROWLAND J. BURGESS ◽  
ADRIAN ALLEN
Keyword(s):  
Amino Acids ◽  
Gastric Mucus ◽  
Mucus Glycoprotein ◽  
Terminal Amino

scholarly journals Food Deprivation Depletes Gastric Mucus Glycoprotein in Streptozotocin-Induced Diabetic Rats

2000 ◽  
Vol 84 (1) ◽  
pp. 51-55 ◽  
Author(s):  
Shigeki Igarashi ◽  
Eisuke Kume ◽  
Hiroshi Narita ◽  
Mine Kinoshita
Keyword(s):  
Food Deprivation ◽  
Diabetic Rats ◽  
Gastric Mucus ◽  
Mucus Glycoprotein

Effect of lipids and proteins on the viscosity of gastric mucus glycoprotein

1984 ◽  
Vol 121 (2) ◽  
pp. 521-529 ◽  
Author(s):  
V.L.N. Murty ◽  
J. Sarosiek ◽  
A. Slomiany ◽  
B.L. Slomiany
Keyword(s):  
Gastric Mucus ◽  
Mucus Glycoprotein
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