The Distribution of Some Enzyme Group Systems Among Marathis and Gujaratis in Bombay

1970 ◽  
Vol 20 (4) ◽  
pp. 409-416 ◽  
Author(s):  
N.M. Blake ◽  
R.L. Kirk ◽  
A.J. Baxi
Keyword(s):  
Enzyme Group

Indole Prenyltransferases from Fungi: A New Enzyme Group with High Potential for the Production of Prenylated Indole Derivatives

2009 ◽  
Vol 16 (2) ◽  
pp. 218-231 ◽  
Author(s):  
N. Steffan ◽  
A. Grundmann ◽  
W.-B. Yin ◽  
A. Kremer ◽  
S.-M. Li
Keyword(s):  
High Potential ◽  
Indole Derivatives ◽  
Enzyme Group

The Distribution of some Enzyme Group Systems Among Parsis and Iranis in Bombay

1972 ◽  
Vol 22 (3) ◽  
pp. 274-282 ◽  
Author(s):  
J.V. Undevia ◽  
N.M. Blake ◽  
R.L. Kirk ◽  
E.M. McDermid
Keyword(s):  
Enzyme Group

scholarly journals Alignment-Free Method to Predict Enzyme Classes and Subclasses

2019 ◽  
Vol 20 (21) ◽  
pp. 5389 ◽  
Author(s):  
Riccardo Concu ◽  
M. Natália D. S. Cordeiro
Keyword(s):  
Classification Scheme ◽  
Quantitative Structure Activity Relationship ◽  
Quantitative Structure ◽  
Numerical Classification ◽  
International Union ◽  
Enzyme Classification ◽  
Alignment Free ◽  
Structure Activity ◽  
Free Model ◽  
Enzyme Group

The Enzyme Classification (EC) number is a numerical classification scheme for enzymes, established using the chemical reactions they catalyze. This classification is based on the recommendation of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. Six enzyme classes were recognised in the first Enzyme Classification and Nomenclature List, reported by the International Union of Biochemistry in 1961. However, a new enzyme group was recently added as the six existing EC classes could not describe enzymes involved in the movement of ions or molecules across membranes. Such enzymes are now classified in the new EC class of translocases (EC 7). Several computational methods have been developed in order to predict the EC number. However, due to this new change, all such methods are now outdated and need updating. In this work, we developed a new multi-task quantitative structure–activity relationship (QSAR) method aimed at predicting all 7 EC classes and subclasses. In so doing, we developed an alignment-free model based on artificial neural networks that proved to be very successful.

The Distribution of Serum Protein and Enzyme Group Systems among North Indians

1971 ◽  
Vol 21 (5) ◽  
pp. 440-457 ◽  
Author(s):  
N.M. Blake ◽  
R.L. Kirk ◽  
E.M. McDermid ◽  
Keiichi Omoto ◽  
Y.R. Ahuja
Keyword(s):  
Serum Protein ◽  
North Indians ◽  
Enzyme Group

scholarly journals Pancreatic Enzyme Supplementation in Acute Pancreatitis

HPB Surgery ◽  
1995 ◽  
Vol 8 (3) ◽  
pp. 159-162 ◽  
Author(s):  
R. V. Patankar ◽  
R. Chand ◽  
C. D. Johnson
Keyword(s):  
Acute Pancreatitis ◽  
Visual Analogue Scale ◽  
Analogue Scale ◽  
Pancreatic Enzyme ◽  
Controlled Study ◽  
Analgesic Requirement ◽  
Double Blind ◽  
Initial Management ◽  
Pain Scores ◽  
Enzyme Group

This study evaluates the effect of oral pancreatic enzyme supplements on pain, analgesic requirement and the incidence of complications in patients with acute pancreatitis. This double blind, prospectively randomised placebo controlled study included 23 patients. Pain was monitored using a visual analogue scale; the analgesic requirement was assessed with a numerical score.No significant differences were noted between the median (range) pain scores of patients who received placebo: 22 (17.1–58) and those who received enzymes: 23 (11.3–63). Hospital stay was 7 (5–10) days in patients on placebo and 8 (6–24) days in the enzyme group (p = 0.069). Analgesic requirements were: placebo 20 (6–60) and enzymes: 16 (0–63) (p = 0.56). This study has shown no beneficial effect of oral pancreatic enzyme supplements in the initial management of patients with acute pancreatitis.

scholarly journals The role of the metal ion in the mechanism of the K+-activated aldehyde dehydrogenase of Saccharomyces cerevisiae

1987 ◽  
Vol 247 (2) ◽  
pp. 377-384 ◽  
Author(s):  
F M Dickinson ◽  
G W Haywood
Keyword(s):  
Metal Ion ◽  
Enzyme Hydrolysis ◽  
Stopped Flow ◽  
Kinetic Measurements ◽  
Step Process ◽  
Catalysed Reaction ◽  
Dehydrogenase Reaction ◽  
Principal Effect ◽  
Enzyme Group

The effect of K+ on assays of the enzyme was studied and it appears that the activation occurs slowly by a two-step process. Kinetic measurements suggest that the enzyme-catalysed reaction can proceed slowly (0.4%) in the complete absence of K+. The enzyme exhibits a K+-activated esterase activity, which is further activated by NAD+ or NADH. Stopped-flow studies indicated that the principal effect of K+ on the dehydrogenase reaction is to accelerate a step (possibly acyl-enzyme hydrolysis) associated with a fluorescence and small absorbance transient that occurs after hydride transfer and before NADH dissociation from the terminal E-NADH complex. The variation of activity of the enzyme with pH was studied. An enzyme group with pKa approx. 7.1 apparently promotes enzyme activity when in its alkaline form.

scholarly journals STUDIES ON THE BACTERIOPHAGES OF HEMOLYTIC STREPTOCOCCI

1958 ◽  
Vol 108 (6) ◽  
pp. 803-821 ◽  
Author(s):  
Richard M. Krause
Keyword(s):  
Cell Walls ◽  
Rabbit Antiserum ◽  
Chemical Properties ◽  
Physical Chemical ◽  
Precipitin Reaction ◽  
Streptomyces Albus ◽  
Serological Reactivity ◽  
Group A ◽  
Almost All ◽  
Enzyme Group

The lysis of cell walls of hemolytic streptococci by a phage-associated lysin has been described. A method is presented for preparing the lysin from Group C streptococcal phage lysates. Following lysis almost all of the cell wall carbohydrate is recovered in solution. This material has the serological reactivity, physical-chemical properties, and values for nitrogen, rhamnose, and glucosamine similar to those of the carbohydrate isolated from the cell walls by the Streptomyces albus enzyme. Group C carbohydrate isolated by either enzyme inactivates Group C bacteriophage. The protein liberated by the lysin from Group A Type 6 cell walls gives a type-specific precipitin reaction with homologous rabbit antiserum. Preliminary data are presented on the ammonium sulfate fractionation and the electrophoretic separation of a protein fraction with the serological reactivity of M protein.

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