Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.21.4 (
trypsin
)
42,187
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The reaction between the three Bowman-Birk proteinase inhibitors isolated from fenugreek seeds (
TFI
-B2,
TFI
-N2 and
TFI
-A8) and the human and bovine proteinases was investigated by studying the complexes formed and their properties.
TFI
-B2, the Lys-Leu
trypsin
chymotrypsin inhibitor, can bind 1.9 mol human
trypsin
(HT), 1.3 mol bovine
trypsin
(BT) and/or 0.4 mol human (HCT) or bovine (BCT) chymotrypsin per mole of inhibitor. HT was bound at the two reactive sites and BT mainly at the lysine-containing
trypsin
-reactive site, whereas HCT and BCT were only bound at the leucine-containing chymotrypsin-reactive site.
TFI
-N2, the Arg-Leu
trypsin
chymotrypsin inhibitor, could bind 1 mol BT and BCT, but 1.3 mol HT and 1.2 mol HCT per mole of inhibitor. In addition to the usual binding, the human enzymes could also be bound at the respective "wrong" reactive site.
TFI
-A8, the Arg-Arg trypsin inhibitor, binds 2 mol HT or BT per mole of inhibitor at the two
trypsin
-reactive sites, whereas HCT and BCT (about 0.2 mol/mol) are bound to one of the two "wrong" reactive sites.
...
PMID:Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigonella foenum-graecum L.) seeds. Reaction with the human and bovine proteinases. 176 94
Three fenugreek inhibitors (
TFI
-A8,
TFI
-N2, and
TFI
-B2) were isolated from an inhibitor preparation by anion exchange chromatography and subsequent preparative isoelectric focusing using immobilized pH gradients and the canal technique. The purified inhibitors inhibited the enzymes tested differently:
TFI
-A8 exhibited a high inhibition of
trypsin
(8.2 mg human
trypsin
/mg and 8.1 mg bovine
trypsin
/mg) and a very low inhibition of chymotrypsin (0.8 mg human chymotrypsin/mg and 1.0 mg bovine chymotrypsin/mg).
TFI
-N2 inhibited the four enzymes to about the same extent (5.0 mg/mg human and 4.1 mg/mg bovine
trypsin
; 4.9 mg/mg human and 3.7 mg/mg bovine chymotrypsin).
TFI
-B2 displayed a high inhibition of
trypsin
(7.5 mg/mg human and 5.1 mg/mg bovine) and a low inhibition of chymotrypsin (1.8 mg/mg human and 1.9 mg/mg bovine). On average, the human enzymes were inhibited better than the bovine ones by the purified inhibitors. The inhibitors contained high amounts of cystine (five or six disulfide bridges per molecule), aspartic acid, threonine, serine and proline, no valine and methionine and two of them also no tryptophan. Their molecular masses were about 6 kDa. Their inclusion into the Bowman-Birk soybean proteinase inhibitor family is discussed.
...
PMID:Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigonella foenum-graecum L.) seeds. Isolation and characterization. 187 34
The reactive sites and the C-terminal sequences of three
trypsin
chymotrypsin inhibitors from fenugreek seeds (
TFI
-B2,
TFI
-N2, and
TFI
-A8) were determined by chemical modification and carboxypeptidase degradation of native und enzymatically modified inhibitors.
TFI
-B2 contained lysine and leucine in the
trypsin
- and chymotrypsin-reactive sites, respectively, and -(Lys)-Phe-Leu-Ile was the C-terminal sequence.
TFI
-N2 possessed arginine and leucine in the
trypsin
- and chymotrypsin-reactive sites, respectively, and -(Tyr)-Lys-Ile-Leu at the C-terminus.
TFI
-A8 contained two arginines, one in each of the two reactive sites. At least one of these sites, although mainly directed against
trypsin
, could also bind some chymotrypsin. -(Leu)-Phe-Ile-Arg was found to be the C-terminus in
TFI
-A8. These results confirmed that all three fenugreek inhibitors belong to the Bowman-Birk proteinase inhibitor family.
...
PMID:Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigonella foenum-graecum L.) seeds. Reactive sites and C-terminal sequences. 196 6
Fenugreek contained proteinase inhibitors inhibiting 5-9 mg human
trypsin
, 5-7 mg bovine
trypsin
, 2-6 mg human chymotrypsin, and 1-3 mg bovine chymotrypsin per g seed material. About 30 inhibitors were electrophoretically detected, and 23 of them, inhibiting all the four enzymes, were characterized by means of their isoelectric points: a group of acid inhibitors (
TFI
-A1 to A10, pI 4.48-5.12), a group of neutral inhibitors (
TFI
-N1 to -N6, pI 5.91-6.71), and a group of basic inhibitors (
TFI
-B1 to -B7, pI 7.76-9.77). To eliminate the galactomannans which complicate further purification, coarsely ground seeds were separated by density into two fractions, seed coats + endosperm and cotyledons + embryos (C + E). Isolation of the fenugreek inhibitors by extraction of fraction C + E, followed by ammonium sulfate fractionation and affinity chromatography on anhydrotrypsin-Sepharose, resulted in an about 700-fold enrichment.
...
PMID:Inhibitors of human and bovine trypsin and chymotrypsin in fenugreek (Trigonella foenum-graecum L.) seeds. Demonstration and purification. 205 14
Ultrasound has been used in dentistry for over 40 years and has recently been proposed for cutting bone. The purpose of this study was to establish the effects of ultrasonic instruments on osteoblasts. A 25 kHz magnetostrictive ultrasound generator and a
TFI
-1 tip (Dentsply, UK) were used as the ultrasound generating instruments. Primary osteoblast cultures were established from the parietal bones of two-day-old Albino Wistar rats grown on tissue culture (TC) petri dishes (Corning, UK) in alphaMEM (Sigma, UK). Once confluent, the osteoblasts were harvested using 0.05%
trypsin
in 0.02% EDTA then 1.7 x 10(5) cells in 2.5 ml of alphaMEM were either re-seeded immediately onto TC dishes and allowed to adhere for 24 h or kept in suspension before application of ultrasound with different tip displacements prior to re-seeding the cells. Osteoblast viability was assessed using 0.4% Trypan Blue following the initial dose of ultrasound then periodically over a 20 h period for both adherent and suspension osteoblasts. This study demonstrated that ultrasound caused osteoblast detachment and loss of viability in vitro, both when adherent to a substrate or in suspension. Loss of osteoblast viability was related to the maximum displacement of the ultrasonic tip and continued throughout the 20 h period observed for osteoblasts adherent to TC dishes.
...
PMID:Osteoblast viability and detachment following exposure to ultrasound in vitro. 1534 54