scholarly journals 1-Deoxynojirimycin Content and Alfa-Glucosidase Inhibitory Activity and Heat Stability of 1-Deoxynojirimycin in Silkworm Powder

2011 ◽  
Vol 02 (02) ◽  
pp. 87-89 ◽  
Author(s):  
Kazuhisa Yatsunami ◽  
Kohji Murata ◽  
Tsutomu Kamei
Keyword(s):  
Inhibitory Activity ◽  
Heat Stability

scholarly journals Bacteriocin-like activity of group B and group C streptococci of human and of animal origin

1983 ◽  
Vol 90 (1) ◽  
pp. 7-18 ◽  
Author(s):  
Christine R. Schofield ◽  
J. R. Tagg
Keyword(s):  
Inhibitory Activity ◽  
Mode Of Action ◽  
Culture Medium ◽  
Heat Stability ◽  
Animal Origin ◽  
Streptococcus Dysgalactiae ◽  
Inhibitory Substance ◽  
Group B Streptococci ◽  
Group B ◽  
Animal Strains

SUMMARYAn inhibitor ‘fingerprinting’ technique was used to test 120 group B and 50 group C streptococcus strains for production of inhibitory activity. The incidence of inhibitor production was low. Five of 70 group B streptococci of animal origin and one of 50 from human sources consistently produced inhibitory activity. Six of 20 animal strains and three of 30 human strains of group C streptococci were inhibitor producers. These included twoStreptococcus dysgalactiae, threeS. equisimilisand fourS. zooepidemicus.The temperature of incubation and species of origin of the blood used in the culture medium were critical determinants of inhibitor production. Investigation of inhibitors for their spectrum of activity, heat stability, sensitivity to trypsin, dialysability and mode of action indicated that five of the group B and seven of the group C streptococci produced inhibitors that had bacteriocin-line properties. Three bovine strains of group B streptococci produced very similar inhibitory activity. A greater variety of bacteriocin-like substances was detected in the group C streptococcus strains. Two of theS. zooepidemicusstrains were each found to Produce more than one inhibitory substance.

scholarly journals Evaluation of Inhibitory Activity, Purification and X-Ray Crystallography of Alpha—Amylase Inhibitor from Phaseolus Vulgaris Cultivars of Uttarakhand

2021 ◽  
Author(s):  
Ravinder Singh ◽  
Anoop Kumar Dobriyal ◽  
Rattan Deep Singh ◽  
Patricio De los Rios-Escalante
Keyword(s):  
Phaseolus Vulgaris ◽  
Crude Extract ◽  
Inhibitory Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Heat Stability ◽  
Alpha Amylase ◽  
Native Page ◽  
X Ray Crystallography ◽  
Amylase Inhibitor ◽  
Alpha Amylase Inhibitor

Abstract The present work is based on analysis of inhibitory activity of alpha-amylase inhibitor in selected cultivars of Phaseolus vulgaris of Uttarakhand. Fifteen samples were assessed for inhibitory activity of alpha-amylase inhibitor. Significant variations were found in different cultivars. Crude extract of alpha-amylase inhibitor from sample PUR (Purola) have shown maximum inhibitory activity (70.2 ± 0.84). Crude extract of all the cultivars have shown considerable variations in inhibitory activity in the temperature ranging from 20ºC to 100ºC. Based on inhibitory activity and heat stability profile, the alpha amylase inhibitor was purified from PUR cultivar. The purified inhibitor was found to be stable even at 90ºC with an inhibitory activity of 97.20 ±0.09. The molecular weight of purified inhibitor on Native PAGE (Polyacrylamide gel electrophoresis) was found to be 31kd, consisting of two subunits of 17kd and 14kd on SDS-PAGE.

scholarly journals The structural basis for neutrophil inactivation of C1̅ inhibitor

1989 ◽  
Vol 258 (1) ◽  
pp. 193-198 ◽  
Author(s):  
P A Pemberton ◽  
R A Harrison ◽  
P J Lachmann ◽  
R W Carrell
Keyword(s):  
Inhibitory Activity ◽  
Limited Proteolysis ◽  
Heat Stability ◽  
Structural Basis ◽  
C1 Inhibitor ◽  
Snake Venoms ◽  
Peptide Bonds ◽  
N Terminus ◽  
Initial Cleavage ◽  
Labile Molecule

Limited proteolysis of C1 inhibitor (C1-INH) by neutrophil elastase, Pseudomonas elastase and snake venoms resulted in initial cleavage within the molecule's N-terminus followed by further cleavage within the molecule's C-terminally placed reactive centre. N-Terminal proteolysis occurred at peptide bonds 14-15, 36-37 and 40-41. This had no effect on either the inhibitory activity or the heat-stability of C1-INH. Proteolysis within the reactive centre occurred at peptide bonds 439-440, 440-441, 441-442 and 442-443. Cleavage at any one of these sites inactivated C1-INH and conferred enhanced heat-stability upon a previously heat-labile molecule. Released neutrophil proteinases also cleaved and inactivated C1-INH, suggesting that they may physiologically regulate C1-INH during inflammatory episodes.

Inhibitory effects of bioaccessible anthocyanins and procyanidins from apple, red grape, cinnamon on α-amylase, α-glucosidase and lipase

2020 ◽  
pp. 1-9
Author(s):  
Pınar Ercan ◽  
Sedef Nehir El
Keyword(s):  
Inhibitory Activity ◽  
Digestive Enzymes ◽  
Positive Control ◽  
Anthocyanin Content ◽  
Inhibitory Effects ◽  
Total Anthocyanin ◽  
Total Anthocyanin Content ◽  
Before And After ◽  
Red Grape

Abstract. The goals of this study were to determine and evaluate the bioaccessibility of total anthocyanin and procyanidin in apple (Amasya, Malus communis), red grape (Papazkarası, Vitis vinifera) and cinnamon (Cassia, Cinnamomum) using an in vitro static digestion system based on human gastrointestinal physiologically relevant conditions. Also, in vitro inhibitory effects of these foods on lipid (lipase) and carbohydrate digestive enzymes (α-amylase and α-glucosidase) were performed with before and after digested samples using acarbose and methylumbelliferyl oleate (4MUO) as the positive control. While the highest total anthocyanin content was found in red grape (164 ± 2.51 mg/100 g), the highest procyanidin content was found in cinnamon (6432 ± 177.31 mg/100 g) (p < 0.05). The anthocyanin bioaccessibilities were found as 10.2 ± 1%, 8.23 ± 0.64%, and 8.73 ± 0.70% in apple, red grape, and cinnamon, respectively. The procyanidin bioaccessibilities of apple, red grape, and cinnamon were found as 17.57 ± 0.71%, 14.08 ± 0.74% and 18.75 ± 1.49%, respectively. The analyzed apple, red grape and cinnamon showed the inhibitory activity against α-glucosidase (IC50 544 ± 21.94, 445 ± 15.67, 1592 ± 17.58 μg/mL, respectively), α-amylase (IC50 38.4 ± 7.26, 56.1 ± 3.60, 3.54 ± 0.86 μg/mL, respectively), and lipase (IC50 52.7 ± 2.05, 581 ± 54.14, 49.6 ± 2.72 μg/mL), respectively. According to our results apple, red grape and cinnamon have potential to inhibit of lipase, α-amylase and α-glucosidase digestive enzymes.

Total synthesis of melleumins A and B and their analogs: Determination of stereochemistry and Wnt signal inhibitory activity

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
M Ishibashi ◽  
S Hanazawa ◽  
Y Uchino ◽  
X Li ◽  
MA Arai
Keyword(s):  
Total Synthesis ◽  
Inhibitory Activity ◽  
Wnt Signal

A QSAR study of macrocyclic diterpenes with P-gp inhibitory activity isolated from Euphorbia species

Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
IJ Sousa ◽  
J Molnar ◽  
MU Ferreira ◽  
MX Fernandes
Keyword(s):  
Inhibitory Activity ◽  
Qsar Study
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