Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of ionizing radiation on the reproduction organs of ewes was studied after single local irradiation of ovaries with different X-ray doses. Twenty two ewes of the Slovak Merino breed at the age of two years and at the average live weight of 30 kg were divided into four test groups to be irradiated with the following doses: Group I (n = 6) 4.78 Gy (500 R), group II (n = 6) 9.67 Gy (1000 R), group III (n = 6) 19.14 Gy (2000 R). The ewes of the fourth group were used as the control; they were only laparotomized, otherwise left intact. The trypsin-inhibiting activity of blood plasma and cervical mucus was determined from the retardation of the hydrolysis of low-molecular substrate (TAPA); the thickness of the epithelium of uterine body and cervix was measured microscopically after fixing and staining. The dynamics of changes in the TIA of cervical mucus, in percentual expression, showed differences when measured in the course of 10, 30 and 100 days (1.84 K, aver. for 1st-10th day: 1 = 2.1; 2 = 1.7; 3 = 1.7; 4 = 2.5. Aver. for 10th-30th days: 1 = 1.8; 2 = 1.7; 3 = 1.8; 4 = 1.0. Aver. for 30th-100th day: 1 = 1.7; 2 = 1.1; 3 = 1.2; 4 = 1.5). The dynamics of changes in the thickness of the epithelium of endometrium, uterine horns and uterine cervix had a different nature. A hundred days from irradiation the values showed little difference.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Dynamic changes in the trypsin-inhibiting activity in cervical mucus, blood and in the histomorphological structure of the uterus in x-irradiated sheep]. 641 37

Four high-yielding varieties of pigeon pea namely UPAS-120, Manak, JCPL-151. ICPL-87 had considerable amounts of antinutrients i.e. saponins and trypsin inhibitors. Saponin content of these unprocessed cultivars ranged from 2164 to 3494 mg/100 g. There were significant varietal variations in trypsin inhibitor activity (1007-1082 TIU/g) of these pigeon pea cultivars. Some simple, inexpensive and easy-to-use domestic processing and cooking methods, namely, soaking (6, 12, 18 h), soaking (12 h)-dehulling, ordinary cooking, pressure cooking and germination (24, 36, 48 h) were found to be quite effective in lowering the level of saponins and trypsin inhibitors in all the pigeon pea cultivars. Pressure cooking of soaked and dehulled seeds lowered the content of saponins to a maximum extent (28 to 38%) followed by ordinary cooking of soaked and dehulled seeds (28 to 35%), soaked dehulled raw seeds (22 to 27%) and 48 h germinated seeds (15 to 19%). Loss of TIA was marginal due to soaking but ordinary as well as pressure cooking of unsoaked and soaked-dehulled pigeon pea seeds reduced the TIA drastically. Pressure cooking of pigeon pea seeds completely destroyed the TIA while it was reduced to the extent of 86-88% against the control in 48 h pigeon pea sprouts.
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PMID:Saponin content and trypsin inhibitor activity in processed and cooked pigeon pea cultivars. 1122 78

Trypsin inhibitors are pathogenesis-related (PR) proteins, which play an important role in the plant defense mechanism against insects and pathogens. Peanut trypsin inhibitors are low molecular mass seed storage proteins. Like peanut allergens, they are stable to acid and heat, resistant to digestion, and can have a negative impact on human health. In peanut, five Bowman-Birk trypsin inhibitors (BBTI) have been isolated and amino acid sequences published. However, to date, no peanut BBTI sequence is available at both the cDNA and the genomic levels. The objectives of this investigation were (i) to synthesize degenerate oligonucleotides based on conserved regions of published amino acid sequences of BBTI, BII, and BIII; (ii) to isolate, sequence, and analyze at least one positive peanut trypsin inhibitor cDNA clone using the synthesized (32)P-labeled oligonucleotides as probes; and (iii) to determine its trypsin inhibitory activity. Thirty-two degenerate oligonucleotides DNA primers of 24 nucleotides each were synthesized based on the published amino acid sequences of peanut BBTI, and two were selected as probes to screen a peanut Lambda gt 11 cDNA library. Three putative positive clones were isolated, purified, and subcloned, and one was sequenced. Sequence analysis revealed a partial cDNA clone of 643 bp with a start codon. This clone shares 93 and 96% nucleotide sequence homology with peanut allergens Ara h 3 and Ara h 4 cDNA clones, respectively. A trypsin inhibitor assay revealed that peanut allergen Ara h 3 has a trypsin inhibitory activity of 11 238 TIA/mg protein. We concluded that peanut allergen Ara h 3 may also function as a trypsin inhibitor.
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PMID:cDNA clone of a putative peanut (Arachis hypogaea L.) trypsin inhibitor has homology with peanut allergens Ara h 3 and Ara h 4. 1499 53

We report for the first time the isolation and characterization of a protease inhibitor from the seeds of Pithecellobium dulce, which is a Leguminosae tree native to Mexico. The purification of the P. dulce trypsin inhibitor (PDTI) was a direct process. After its extraction (pH 8.0) and precipitation (80% (NH(4))(2)SO(4)), the pH was adjusted to 4.0, the supernatant was loaded onto a CM-Sepharose column, and a single peak of trypsin inhibitory activity was eluted (CM-TIA). The main component of CM-TIA was PDTI, a protein composed of two polypeptide chains joined by disulfide bridge(s), with a pI of 4.95 and a molecular weight determined by electrospray mass spectrometry of 19 614 Da. The N-terminal sequence of PDTI has the highest similarity with the seed inhibitor of Acacia confusa. PDTI lacks chymotrypsin inhibitory activity. A low rate of cytotoxicity of CM-TIA toward RINm5F cells contrasted with a high rate of the active fraction G75-TIA (gel filtration chromatography; LC(50) of 0.04 mg/mL).
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PMID:Isolation and properties of a Kunitz-type protein inhibitor obtained from Pithecellobium dulce seeds. 1545 75

In this study trypsin (TIA) and chymotrypsin inhibitory (CIA) activities were determined in the extracts of wheat, rye mix, mixed cereals and, whole wheat flours and, breads made with these flours. In addition, effects of fermentation, baking and in vitro digestion on TIA and CIA were studied. Whole wheat flour, dough, and bread did not show any TIA. Other flours displayed TIA. Contrary to, all flours, doughs, and breads exhibited CIA. Although TIA was not detected in the protein extracts obtained from wheat and rye mix breads, protein extract of rye mix flour exhibited TIA. Following in vitro digestion process, TIA of wheat bread was found as 5.91units/mL gastric dialysate and 9.17units/mL intestine dialysate. CIA was determined in dialysates obtained from wheat (2.12CI/mL and 3.78CI/mL for gastric and intestinal dialysate respectively) and rye breads (4.16CI/mL and 2.46CI/mL for gastric and intestinal dialysate respectively).
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PMID:Protease inhibitors in various flours and breads: Effect of fermentation, baking and in vitro digestion on trypsin and chymotrypsin inhibitory activities. 2815 94