Partial Hydrolysis Products Derived from Proteins and their Significance for Protein Structure.

1943 ◽  
Vol 32 (1) ◽  
pp. 135-172 ◽  
Author(s):  
R. L. M. Synge
Keyword(s):  
Protein Structure ◽  
Partial Hydrolysis ◽  
Hydrolysis Products

Ketoximate Derivatives of Titanium Alkoxides and Partial Hydrolysis Products Thereof

2009 ◽  
Vol 2009 (22) ◽  
pp. 3333-3340 ◽  
Author(s):  
Stefan O. Baumann ◽  
Maria Bendova ◽  
Helmut Fric ◽  
Michael Puchberger ◽  
Claudia Visinescu ◽  
...  
Keyword(s):  
Partial Hydrolysis ◽  
Titanium Alkoxides ◽  
Hydrolysis Products ◽  
Derivatives Of

scholarly journals A Novel Agarase, Gaa16B, Isolated from the Marine Bacterium Gilvimarinus agarilyticus JEA5, and the Moisturizing Effect of Its Partial Hydrolysis Products

Marine Drugs ◽  
2021 ◽  
Vol 20 (1) ◽  
pp. 2
Author(s):  
Youngdeuk Lee ◽  
Eunyoung Jo ◽  
Yeon-Ju Lee ◽  
Tae-Yang Eom ◽  
Yehui Gang ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Average Molecular Weight ◽  
Biochemical Properties ◽  
Partial Hydrolysis ◽  
Carbohydrate Binding ◽  
Thin Layer Chromatography Analysis ◽  
Amino Acid Similarity ◽  
Chromatography Analysis ◽  
Hydrolysis Products ◽  
Layer Chromatography

We recently identified a β-agarase, Gaa16B, in the marine bacterium Gilvimarinus agarilyticus JEA5. Gaa16B, belonging to the glycoside hydrolase 16 family of β-agarases, shows less than 70.9% amino acid similarity with previously characterized agarases. Recombinant Gaa16B lacking the carbohydrate-binding region (rGaa16Bc) was overexpressed in Escherichia coli and purified. Activity assays revealed the optimal temperature and pH of rGaa16Bc to be 55 ∘C and pH 6–7, respectively, and the protein was highly stable at 55 ∘C for 90 min. Additionally, rGaa16Bc activity was strongly enhanced (2.3-fold) in the presence of 2.5 mM MnCl2. The Km and Vmax of rGaa16Bc for agarose were 6.4 mg/mL and 953 U/mg, respectively. Thin-layer chromatography analysis revealed that rGaa16Bc can hydrolyze agarose into neoagarotetraose and neoagarobiose. Partial hydrolysis products (PHPs) of rGaa16Bc had an average molecular weight of 88–102 kDa and exhibited > 60% hyaluronidase inhibition activity at a concentration of 1 mg/mL, whereas the completely hydrolyzed product (CHP) showed no hyaluronidase at the same concentration. The biochemical properties of Gaa16B suggest that it could be useful for producing functional neoagaro-oligosaccharides. Additionally, the PHP of rGaa16Bc may be useful in promoting its utilization, which is limited due to the gel strength of agar.

scholarly journals STUDIES ON THE PRECIPITIN REACTION

1933 ◽  
Vol 57 (3) ◽  
pp. 373-379 ◽  
Author(s):  
Michael Heidelberger ◽  
Forrest E. Kendall
Keyword(s):  
Structural Unit ◽  
Horse Serum ◽  
Partial Hydrolysis ◽  
Specific Inhibition ◽  
Type Iii ◽  
Hydrolysis Products ◽  
Precipitin Reaction ◽  
Specific Polysaccharide

1. Partial hydrolysis products of the specific polysaccharide of Type III pneumococcus ranging from 550 to 1,800 in formula weight can be quantitatively freed from unhydrolyzed polysaccharide. 2. The fractions yield specific precipitates with Type III antipneumococcus horse serum but fail to precipitate homologous rabbit antisera, giving rise only to specific inhibition. The aldobionic acid, the structural unit of S III, does not precipitate antisera. 3. A possible explanation and a possible application of the findings are pointed out.

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