Identification and Partial Characterization of Trypsin Inhibitory Activity in Seed of Some Fruit Plants

2010 ◽  
Vol 19 (2) ◽  
pp. 235-237 ◽  
Author(s):  
Deepankar Gahloth ◽  
Ashwani Kumar Sharma
1980 ◽  
Vol 188 (1) ◽  
pp. 145-152 ◽  
Author(s):  
F De Matteis ◽  
A H Gibbs ◽  
T R Tephly

1. A modified porphyrin with inhibitory activity towards protohaem ferro-lyase was purified from the livers of mice treated with 3,5-diethoxycarbonyl-1,4-dihydrocollidine, and partially characterized. 2. The inhibitor can be labelled by 5-amino[4-14C]-laevulinate, suggesting that it originates from pre-labelled liver haem. No radioactivity from 3,5-diethoxycarbonyl-1,4-dihydro[2,6-14C]collidine can be recovered bound to the purified abnormal porphyrin when the radioactive drug is used to induce its formation. 3. Similar modified porphyrins isolated from the livers of animals treated with 2-allyl-2-isopropylacetamide, secobarbitone or 1-ethynylcyclohexanol did not exhibit inhibitory activity toward protohaem ferro-lyase. 4. The inhibition of protohaem ferro-lyase was progressive, could be slowed down by cooling and partially prevented by preincubating the enzyme with the porphyrin substrate. Once established, inhibition could not be reversed by addition of the substrate 5. These results suggest that the modified porphyrin irreversibly inhibits protohaem ferro-lyase and may be used as a sensitive and selective reagent to titrate the number of active centres of the enzyme.


2009 ◽  
Vol 16 (12) ◽  
pp. 1557-1564 ◽  
Author(s):  
Maria das Gracas Freire ◽  
Ilka Vasconcelos ◽  
Marcos Oliveira ◽  
Goncalo de Souza Filho ◽  
Maria Ligia Macedo

1986 ◽  
Vol 56 (03) ◽  
pp. 349-352 ◽  
Author(s):  
A Tripodi ◽  
A Krachmalnicoff ◽  
P M Mannucci

SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Affinity adsorption of the propositus’ plasma to human α-thrombin immobilized on sepharose beads revealed defective binding of the anti thrombin III to thrombin-sepharose. Hence the molecular defect of this variant appears to be at the active site responsible for binding and neutralizing thrombin, thus accounting for the low thrombin inhibitory activity.


2010 ◽  
Vol 108 (10) ◽  
pp. 323-329 ◽  
Author(s):  
Marti F. A. Bierhuizen ◽  
Moniek de Wit ◽  
Carin A. R. L. Govers ◽  
Willem van Dijk

1966 ◽  
Vol 241 (7) ◽  
pp. 1530-1536
Author(s):  
Marcos Rojkind ◽  
Olga O. Blumenfeld ◽  
Paul M. Gallop

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