Ontogenic development of enzymatic activity and digestive system in Jullien's golden carp (Probarbus jullieniSauvage, 1880)

2018 ◽  
Vol 49 (10) ◽  
pp. 3362-3373 ◽  
Author(s):  
Ubonrat Limtipsuntorn ◽  
Wikrom Rungsin ◽  
Karun Thongprajukaew ◽  
Wiwihthanon Boonyung ◽  
Wannapa Rangsin
Keyword(s):  
Enzymatic Activity ◽  
Digestive System ◽  
Ontogenic Development ◽  
Golden Carp

scholarly journals Influence of dietary fatty acid composition on enzymatic activity and digestive histology in silver catfish (Rhamdia quelen)

2021 ◽  
Vol 10 (3) ◽  
pp. e26010312530
Author(s):  
Suzete Rossato ◽  
João Radünz Neto ◽  
Alexandra Pretto ◽  
Isadora Liberalesso de Freitas ◽  
Eduardo Cargnin Ferreira ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Lipid Profile ◽  
Digestive Tract ◽  
Digestive Enzymes ◽  
Digestive System ◽  
Soybean Protein ◽  
Dietary Fatty Acids ◽  
Histological Techniques ◽  
Silver Catfish ◽  
First Feeding

Dietary fatty acids may influence the development of the digestive tract and initial activation of digestive enzymes in fish. The objective of this study was to evaluate the effect of the diet lipid profile on ontogeny and activity of digestive enzymes in silver catfish post larvae fed practical diets. Five diets were tested, replacing broiler liver by soybean protein concentrate (SPC) or fish meal (FM): Standard, 15SPC, 30SPC, 15FM and 30FM. The enzymatic activity of fish was analyzed from 32 Hours after fertilization (Haf). Were analysed acid protease, trypsin, chymotrypsin, lipase, amylase and maltase. The development of the digestive system was analyzed from first feeding up to 28 days by histological techniques. The enzymatic activity presented peaks for the post-larvae fed with the 15SPC diet and fish fed with diet 15FM showed best growth. The development of the digestive system did not suffer damage from the diets offered. Post-larvae fed the 30SPC diet showed reduced development of the digestive tract. The diet 15FM provide good lipid profile for silver catfish post larvae.

A Method for the Colorimetric Determination of β-Glucuronidase in Urine, Serum, Tissue; Assay of Enzymatic Activity in Health and Disease

1959 ◽  
Vol 36 (2) ◽  
pp. 193-201 ◽  
Author(s):  
Julius A. Goldbarg ◽  
Esteban P. Pineda ◽  
Benjamin M. Banks ◽  
Alexander M. Rutenburg
Keyword(s):  
Enzymatic Activity ◽  
Colorimetric Determination ◽  
Health And Disease ◽  
Urine Serum

Isolation of Antithrombin III from Normal and α1-Antitrypsin-Deficient Human Plasma

1977 ◽  
Vol 38 (02) ◽  
pp. 0475-0485 ◽  
Author(s):  
Anna D. Borsodi ◽  
Ralph A. Bradshaw
Keyword(s):  
Enzymatic Activity ◽  
Isoelectric Focusing ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Antithrombin Activity ◽  
Bovine Trypsin ◽  
Normal Plasma ◽  
Antitrypsin Deficiency ◽  
Simplified Procedure ◽  
Stimulation Of

SummaryThe plasma of individuals, hetero- or homozygous for α1-antitrypsin deficiency, contains greatly decreased amounts of antithrombin activity as assayed against factor Xa. However, heparin stimulation of the residual antithrombin activity is observed, which is comparable to that of normal plasma. Antithrombins isolated from both normal and α1-antitrypsin deficient plasma by a simplified procedure are indistinguishable in both properties and yields. The microheterogeneity observed on isoelectric focusing of both preparations can be eliminated by treatment with neuraminidase. Neither purified human antithrombin nor α1-antitrypsin, when assayed against bovine trypsin, is stimulated by heparin. These results clearly establish the unique natures of antithrombin and α1-antitrypsin and show that about 75% of the antithrombin activity measured in normal plasma is due to α1-antitrypsin. Estimates of anti thrombin III activity in normal plasma by assays dependent on enzymatic activity can probably be obtained only in the presence of heparin.

Mechanism of Inhibitory Action on Platelet Activation of a Phospholipase A2 Isolated from Lachesis muta (Bushmaster) Snake Venom

1997 ◽  
Vol 78 (05) ◽  
pp. 1372-1380 ◽  
Author(s):  
André L Fuly ◽  
Olga L T Machado ◽  
Elias W Alves ◽  
Célia R Carlinis
Keyword(s):  
Platelet Aggregation ◽  
Enzymatic Activity ◽  
Phospholipase A2 ◽  
Inhibitory Activity ◽  
Thermal Inactivation ◽  
Anticoagulant Activity ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Crude Venom ◽  
Lachesis Muta

SummaryCrude venom from Lachesis muta exhibited procoagulant, proteolytic and phospholipase A2 activities. A phospholipase A2, denoted LM-PLA2 was purified from L. muta venom to homogeneity, through a combination of chromatographic steps involving gel-filtration on Sephacryl S-200 HR and reverse phase chromatography on a C2/C18 column. LM-PLA2 presented a single polypeptide chain with an isoelectric point at pH 4.7 and apparent molecular weight of 17 kDa. Partial aminoacid sequence indicated a high degree of homology for LM-PLA2 with other PLA2 from different sources.LM-PLA2 displayed a potent enzymatic activity as measured by indirect hemolysis of red blood cells but it was neither lethal when injected i.p. into mice nor did it present anticoagulant activity. Furthermore, LM-PLA2 displayed a moderate inhibitory activity on the aggregation of rabbit platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, platelet aggregation induced by high doses of collagen was strongly inhibited by LM-PLA2 as well as ATP-release. Treatment of the protein with p-bromophenacyl bromide or 2-mercapto-ethanol, as well as thermal inactivation studies, suggested that the platelet inhibitory effect of LM-PLA2 is dependent on its enzymatic activity. Thus, the platelet inhibitory activity of LM-PLA2 was shown to be dependent on the hydrolysis of plasma phospholipids and/or lipoproteins, most probably those rich in phosphatidylcholine. Surprisingly, lyso-phosphatidylcholine released by LM-PLA2 from plasma was shown to preferentially inhibited collagen-induced platelet aggregation, in contrast to other PLA2s, whose plasma hydrolytic products indistinctly affect platelet’s response to several agonists.

Degradation of 2,4-dichlorophenol by melamine amine celluloseimmobilized lacasses

TAPPI Journal ◽  
2017 ◽  
Vol 16 (10) ◽  
pp. 559-564 ◽  
Author(s):  
ZHEN WANG ◽  
PINGPING BIN ◽  
YING LIU ◽  
YU LIU ◽  
GUIHUA YANG ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Removal Efficiency ◽  
Immobilized Laccase ◽  
Dialdehyde Cellulose

Epoxidized dialdehyde cellulose (EDC) was prepared and grafted with melamine to obtain melamine grafted epoxidized dialdehyde cellulose (EDC-melamine); the products were characterized by various methods and were used as carriers to immobilize laccase. Results show EDC-melamine can immobilize laccase effectively and have higher enzymatic activity compared with EDC. Furthermore, the enzymatic activity of EDC-melamine was found to be as high as 865 U•mg-1, compared with 140U•mg-1 for EDC. The removal efficiency of 2,4-dichlorophenol (2,4-DCP) for EDC-melamine immobilized laccase was about 71.5% at 40°C for 4 h at 10.0 mg•L-1 and dosage of laccase = 0.2 g/L. The removal efficiency can remain greater than 63%, even after six cycles.

Digestive system diseases associated with Turner's syndrome in 3 pediatric cases

2018 ◽  
Author(s):  
Lamia Gargouri ◽  
Faten Hadjkacem ◽  
Dorra Ghorbel ◽  
Faiza Safi ◽  
Manel Hsairi ◽  
...  
Keyword(s):  
Digestive System ◽  
Turner's Syndrome ◽  
Turner’S Syndrome ◽  
Digestive System Diseases
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