scholarly journals Chemical modification of arginine residues of lung galaptin and fibronectin. Effects on fibroblast binding

1985 ◽  
Vol 232 (3) ◽  
pp. 919-922 ◽  
Author(s):  
J T Powell
Keyword(s):  
Chemical Modification ◽  
Lung Fibroblasts ◽  
Plasma Fibronectin ◽  
Cell Binding ◽  
Lectin Activity ◽  
Marked Diminution ◽  
Arginine Residues

Lung galaptin bound to lung fibroblasts with a Kd of 190 nM, and this binding could be inhibited by 20 mM-lactose. Selective modifications of the arginine residues of galaptin with cyclohexane-1,2-dione did not change its lectin activity or its binding to fibroblasts. By contrast, modification of the arginine residues of plasma fibronectin resulted in a marked diminution of protein-fibroblast binding. Selective modification of arginine residues may provide a useful probe for -Arg-Gly-Asp-Xaa cell-binding sequences of proteins.

scholarly journals Chemical modification studies on a lectin from Saccharomyces cerevisiae (baker's yeast)

1987 ◽  
Vol 244 (3) ◽  
pp. 579-584 ◽  
Author(s):  
M Kundu ◽  
J Basu ◽  
A Ghosh ◽  
P Chakrabarti
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Chemical Modification ◽  
Binding Site ◽  
Structural Changes ◽  
Thiol Groups ◽  
Lectin Activity ◽  
Partial Protection ◽  
Sugar Binding ◽  
Arginine Residues ◽  
Glycine Ethyl Ester

The effect of chemical modification on a galactose-specific lectin isolated from a fatty acid auxotroph of Saccharomyces cerevisiae was investigated in order to identify the type of amino acids involved in its agglutinating activity. Modification of 50 free amino groups with succinic anhydride or citraconic anhydride led to an almost complete loss of activity. This could not be protected by the inhibitory sugar methyl alpha-D-galactopyranoside. Treatment with N-bromosuccinimide and N-acetylimidazole, for the modification of tryptophan and tyrosine residues, did not affect lectin activity. Modification of carboxy groups with glycine ethyl ester greatly affected lectin activity, although sugars afford partial protection. Modification of four thiol groups with N-ethylmaleimide was accompanied by a loss of 85% of the agglutinating activity, and two thiol groups were found to be present at the sugar-binding site of the lectin. Modification of 18 arginine residues with cyclohexane-1,2-dione and 26 histidine residues with ethoxyformic anhydride led to a loss of lectin activity. However, in these cases, modification was not protected by the abovementioned inhibitory sugar, suggesting the absence of these groups at the sugar-binding site. In all the cases, immunodiffusion studies with modified lectin showed no gross structural changes which could disrupt antigenic sites of the lectin.

Chemical modification of the functional arginine residues of carbon monoxide dehydrogenase from Clostridium thermoaceticum

Biochemistry ◽  
1989 ◽  
Vol 28 (17) ◽  
pp. 7112-7116 ◽  
Author(s):  
T. Shanmugasundaram ◽  
Ganesh K. Kumar ◽  
Bhami C. Shenoy ◽  
Harland G. Wood
Keyword(s):  
Carbon Monoxide ◽  
Chemical Modification ◽  
Carbon Monoxide Dehydrogenase ◽  
Clostridium Thermoaceticum ◽  
Arginine Residues

Essential Arginine Residues in Lactate Dehydrogenase from Germinating Soybean

1994 ◽  
Vol 59 (2) ◽  
pp. 467-472 ◽  
Author(s):  
Jana Barthová ◽  
Irena Hulová ◽  
Miroslava Birčáková
Keyword(s):  
Enzyme Activity ◽  
Glycine Max ◽  
Lactate Dehydrogenase ◽  
Chemical Modification ◽  
Active Site ◽  
Enzyme Modification ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
Arginine Residues ◽  
Blue Sepharose

The lactate dehydrogenase was isolated from soybean (Glycine max. L.) by a procedure that employed biospecific chromatography on a column of Blue-Sepharose CL-6B. The participation of the guanidine group of arginine residues in the mechanism of enzyme action was determined through kinetic and chemical modification studies. The dependence of enzyme activity on pH was followed in the alkaline region (pH 8.6 - 12.8). The pK values found were 12.4 for the enzyme substrate complex and 11.1 for the free enzyme. The enzyme was inactivated by phenylglyoxal, 2,3-butanedione, 1,2-cyclohexanedione and p-hydroxyphenylglyoxal reagents used in modification experiments. Kinetic analysis of the modification indicated that one arginine residue is modified when inactivation occurs. No effect was observed on the rate of inactivation upon addition of coenzyme. The extent of enzyme modification by p-hydroxyphenylglyoxal was determined. It appears there are at least two arginine residues in the active site of the enzyme.

Effect of Lectins and Chemical Modification on the Hemagglutinin Activity of Human Plasma Fibronectin

1981 ◽  
Vol 36 (9-10) ◽  
pp. 863-868 ◽  
Author(s):  
Matti Vuento ◽  
Eija Salonen
Keyword(s):  
Chemical Modification ◽  
Human Plasma ◽  
Present Report ◽  
Red Cells ◽  
Carboxyl Groups ◽  
Plasma Fibronectin ◽  
Cell Surfaces ◽  
Serum Factors ◽  
Low Concentrations ◽  
Erythrocyte Surface

Abstract Purified hum an plasm a fibronectin has been shown to agglutinate protease-treated red cells [Vuento, Hoppe-Seyler's Z. Physiol. Chem. 360, 1327-1333, (1979)]. The present report shows that the activity is inhibited by low concentrations of lectins and by macrom olecular serum factors. Chemical m odification of carboxyl groups of fibronectin strongly inhibited the activity, but modification of am ino groups or guanidinium groups had little effect on the activity. The results suggest that fibronectin receptors on erythrocyte surface are carbohydrate-containing molecules. Humoral m acrom olecular factors may control the interaction of fibronectin with cell surfaces. Chemical m odification studies indicate that the parts of the fibronectin molecule responsible for the hem agglutinin activity are different from those mediating the binding of fibronectin to collagen.

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