Characterization of an acid hydrolysis product of starfish toxins as a 5.alpha.-pregnane derivative

1972 ◽  
Vol 94 (11) ◽  
pp. 4051-4052 ◽  
Author(s):  
Yuzuru Shimizu
Keyword(s):  
Acid Hydrolysis ◽  
Hydrolysis Product

PREPARATION AND CHARACTERIZATION OF SUGARCANE BAGASSE NANOCELLULOSE CRYSTALLINE USING ACID HYDROLYSIS WITH AND WITHOUT ULTRASONICATION

2021 ◽  
Vol 14 (01) ◽  
pp. 601-607
Author(s):  
N.A. Sri Aprilia ◽  
S. Mulyati ◽  
P.N. Alam ◽  
N. Razali ◽  
Zuhra ◽  
...  
Keyword(s):  
Acid Hydrolysis ◽  
Sugarcane Bagasse

Characterization of two Salmonella newport bacteriophages

1979 ◽  
Vol 25 (9) ◽  
pp. 1063-1072 ◽  
Author(s):  
N. Moazamie ◽  
H.-W. Ackermann ◽  
M. R. V. Murthy
Keyword(s):  
Molecular Weight ◽  
Melting Point ◽  
Acid Hydrolysis ◽  
Phage Particle ◽  
Size Classes ◽  
Salmonella Newport ◽  
Double Stranded Dna

Salmonella newport phages 16–19 and 7–11 have very long heads and are members of two rare and so far little-known phage groups. Both produce various morphological aberrations. Preparations of phage 7–11 contain numerous polyheads and about 0.4% short heads belonging to nine size classes. In addition, one giant phage particle was observed. The head of phage 7–11 seems to be an icosahedron which became elongated by adding successive rows of subunits. Phages 16–19 and 7–11 have buoyant densities in CsCl of 1.43 and 1.48 g/mL and particle weights of 103 and 204 × 106 respectively. Both viruses contain double-stranded DNA, internal proteins, and sugars. Phage 16–19 contains 46.5% DNA of 35 × 106 molecular weight, and glucose. Phage 7–11 contains 47.5% DNA of 108 × 106 molecular weight, and mannose. Base compositions of phage and S. newport DNAs were determined from buoyant densities, melting point, and acid hydrolysis. Phage 16–19 contains 5.4% 5-methylcytosine.

Characterization of lignins from Populus alba L. generated as by-products in different transformation processes: Kraft pulping, organosolv and acid hydrolysis

2019 ◽  
Vol 126 ◽  
pp. 18-29 ◽  
Author(s):  
Raquel Martín-Sampedro ◽  
José I. Santos ◽  
Úrsula Fillat ◽  
Bernd Wicklein ◽  
María E. Eugenio ◽  
...  
Keyword(s):  
Acid Hydrolysis ◽  
Kraft Pulping ◽  
Populus Alba ◽  
Transformation Processes ◽  
By Products

Isolation and Characterization of a Chlorogenic Acid Esterase from Aspergillus niger

1980 ◽  
Vol 35 (3-4) ◽  
pp. 209-212 ◽  
Author(s):  
B. Schöbel ◽  
W. Pollmann
Keyword(s):  
Enzyme Activity ◽  
Chlorogenic Acid ◽  
Divalent Cations ◽  
Hydrolysis Product ◽  
The Other ◽  
Temperature Optimum ◽  
Pig Liver ◽  
Isolation And Characterization

Abstract The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum were 6.5 and 45 °C respectively. Divalent cations were not required for the enzyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. The Km-value is 0.70 mᴍ chlorogenic acid, the molecular weight 240000. The described enzyme is specific for chlorogenic acid. On the other hand a typical unspecific esterase like the pig liver esterases does not split chloro­genic acid. The isoelectric focusing reveals several isoenzymes of chlorogenase within a pI-range of 4.0-4.5.

scholarly journals Inactivation of cysteine proteases by peptidyl epoxides: characterization of the alkylation sites on the enzyme and the inactivator

2000 ◽  
Vol 346 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Amnon ALBECK ◽  
Sharon KLIPER
Keyword(s):  
Model Compound ◽  
Hydrolysis Product ◽  
Cysteine Proteases ◽  
Cysteine Residue ◽  
High Resolution Mass Spectrum ◽  
Mass Spectral Analysis ◽  
Mass Spectral ◽  
13C Nmr Analysis ◽  
Unique Signal

Erythro peptidyl epoxides are selective inactivators of cysteine proteases. The alkylation site, both on the enzyme papain and on the epoxide itself, was characterized. The inactivation of papain with the peptidyl epoxide erythro benzyloxycarbonyl-Phe-Ala-epoxide was followed by total hydrolysis by acid. Mass spectral analysis of the hydrolysate revealed, in addition to the expected amino acids, a unique signal of m/z 209 (MH+). Its high-resolution mass spectrum and daughter peak analysis correspond to the product of alkylation on cysteine and the expected fragmentation. A similar MS pattern was obtained for a synthetic model compound corresponding to the expected hydrolysis product. A 13C NMR analysis of papain inactivated by a specifically 13C-labelled peptidyl epoxide indicated that the alkylation of the enzyme's cysteine residue occurs on the primary carbon of the epoxide moiety.

Preparation and characterization of starch nanocrystals combining ball milling with acid hydrolysis

2018 ◽  
Vol 180 ◽  
pp. 122-127 ◽  
Author(s):  
Limin Dai ◽  
Changwei Li ◽  
Jun Zhang ◽  
Fang Cheng
Keyword(s):  
Acid Hydrolysis ◽  
Ball Milling ◽  
Starch Nanocrystals
Sign in / Sign up

Export Citation Format

Share Document