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

To eliminate highly antigenic substances, bovine pericardium was washed in 5% sodium chloride (NaCl) for 24 hours, followed by incubation in trypsin for 40 minutes. To achieve adequate fixation, NaCl-trypsin-treated pericardium was preserved in glutaraldehyde (GA) solution with gradually increasing concentrations from 0.1% to 0.25%. To inactivate the free aldehyde groups and residual GA on the surface of the implant, NaCl-trypsin-GA-treated pericardial samples were posttreated separately with 1% lysine, 8% monosodium glutamate, and 4% chitosan. Fresh (untreated) and 0.1%, 0.2%, and 0.625% GA-treated and NaCl-trypsin-GA-treated pericardial specimens were prepared for comparative study. All samples were implanted subdermally in rats for 2, 4, 8, and 12 weeks for calcification studies. Morphologic and chemical analyses showed mild calcification in fresh pericardia (Ca, 10.5 +/- 1.25 micrograms/mg, von Kossa +) and in glutamate-posttreated pericardia (Ca, 11.5 +/- 3.45 micrograms/mg, von Kossa +). Calcium was practically undetectable in chitosan-posttreated implants (Ca, 1.1 +/- 0.27 micrograms/mg, von Kossa 0), whereas severe calcification was noticed in the rest of the samples (mean Ca greater than 200.0 micrograms/mg, von Kossa ) at 12 weeks. This study suggests that posttreatment with an amino compound such as chitosan would prevent the calcification of GA-treated bioprostheses at an early implantation stage, but elimination of antigenic factors and adequate GA fixation would prevent tissue degeneration, thus enabling the prosthesis to function over a long period.
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PMID:Prevention of calcification of heart valve bioprostheses: an experimental study in rat. 764 84

In this study an attempt was made to find an optimum method of chemical treatment to prevent the calcification of bioprosthetic heart valves. Bovine pericardium was washed in a 5% sodium chloride solution followed by trypsin (Tr) treatment and was kept in 0.1% glutaraldehyde (GA) with a gradual increase in concentration up to 0.25% GA and finally posttreated with a 4% chitosan (Ch) solution. Fresh, 0.2% GA, 0.625% GA, and sodium chloride-Tr-GA treated pericardial samples were taken for comparative study. Tensile testing showed comparable strength and elongation at the breaking point for all groups. The thermal shrinkage studies indicated merit of the proposed treatment (5% sodium chloride-trypsin-glutaraldehyde treated pericardia with chitosan and without chitosan posttreatment). Collagenase assay showed that all differently treated (GA) materials were equally resistant to collagenase. All samples were implanted subcutaneously in rats for 2, 4, 8, or 12 weeks for calcification study. Morphological and mineral analyses showed complete prevention of calcification in sodium chloride-trypsin-GA-chitosan treated pericardium (Ca was 1.1 +/- 0.27 mg/g, von Kossa 0) at the 12th week of implantation.
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PMID:Prevention of calcification of tissue valves. 783 57

The aim of the present study was to develop a chemical treatment to eliminate highly antigenic substances, to standardize the glutaraldehyde fixation procedure, to determine the dominant factors contributing to the calcification process and to understand the role of macromolecules like chitosan in the prevention of calcification of bioprosthetic heart valves. Bovine pericardium treated with 5% sodium chloride-trypsin-glutaraldehyde (GA)-chitosan did not calcify at 12 wk in the rat (calcium, 1.1 +/- 0.27 mg/g; von Kossa, 0). Slow release of residual GA from the bioprosthesis and free aldehyde groups on that are still considered the dominant factors for enhancing calcification of GA-treated bioprostheses.
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PMID:Anticalcification treatment of pericardial prostheses. 808 Sep 38

Peptides such as somatostatin (SS14), epidermal growth factor (EGF), transforming growth factor-alpha (TGF alpha), and insulin-like growth factors (IGF-I and IGF-II) are present in breast milk from various species, and their significance in the developing gastrointestinal tract has been suggested. Our recent studies have indicated that rat milk soluble fraction (RMSF) protects SS14 in the gastrointestinal lumen by inhibiting in vitro the luminal peptidolysis. In the present studies, we have shown that RMSF inhibited in vitro degradation by midjejunal luminal flushings of suckling rats of 125I-labeled somatostatin 14[Tyr11], EGF, TGF alpha, IGF-I and IGF-II, as well as trypsin activity in vitro against benzoyl-L-arginyl-p-nitroanilide. The inhibitory factors present in the RMSF were further fractionated by gel filtration on Sephadex G100, ion-exchange chromatography on DEAE-Sephadex, and fast protein liquid chromatography (FPLC). Gel filtration of Sephadex G100 separated RMSF into three peaks of proteins: G1, G2, and G3; peptidase inhibitor activities were present exclusively in G1. Ion-exchange chromatography on DEAE-Sephadex column resolved peptidase inhibitory activity (G1) into three different peaks, D1, D2, and D3, eluted at sodium chloride concentrations of 0.05 M, 0.1 M, and 0.2 M, respectively. Further purification of D2 by FPLC resulted in a fraction rich in peptidase inhibitory activity, which was essentially free of trypsin inhibitory activity. Results indicate the presence of at least three peptidase inhibitors in rat milk, which may play a role in the protection of milk-borne peptides in the gastrointestinal lumen.
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PMID:Presence of multiple forms of peptidase inhibitors in rat milk. 814 98

The purpose of this study was to determine whether encapsulation of vasoactive intestinal peptide (VIP) in liposomes enhances its vasoactive effects. Liposomes were formed from a solution of VIP in phospholipids and cholesterol, resulting in incorporation of 0.008 mole peptide/mole phospholipid. Leakage of VIP from the liposomes was undetectable over several days of incubation at 4 degrees C in 0.15 M sodium chloride. Under conditions permitting rapid hydrolysis of VIP by trypsin, there was no breakdown of the encapsulated peptide. Increasing concentrations of the liposome-encapsulated VIP administered intravenously to anesthetized hamsters produced a concentration-dependent decrease in the mean arterial blood pressure. The duration and magnitude of the hypotensive effect of the encapsulated VIP was significantly greater (p < 0.05) compared to equivalent concentrations of the unencapsulated peptide. Infusion of empty liposomes was without significant effect on the mean arterial blood pressure. We conclude that encapsulation of VIP in liposomes potentiates the blood pressure-lowering effect of the peptide.
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PMID:Vasoactive intestinal peptide encapsulated in liposomes: effects on systemic arterial blood pressure. 815 24

Glutaraldehyde (GA)-pretreated gentamicin post-fixed bovine pericardium has been evaluated as a wound dressing in this study. Two excisions approximately 7 x 4 cm, each of full thickness skin, from the upper and lower parts down to, but not including, the panniculus carnosus were made from the back of the guinea pig. The skin excised from the upper part was placed on the wound bed of the lower part as an autograft, whereas the upper wound was closed using 5% sodium chloride-trypsin-0.1% GA-0.048% gentamicin-treated bovine pericardium and sutured for comparative study. The wounds were inspected every 3-6 d for infection and exudation. Histopathological studies were performed at weekly intervals in the post-operative period. At the fifth week, a very thin linear scar on the epidermal aspect without remarkable contracture was observed and histopathology showed the completion of epithelization across the wounds in all cases. This study demonstrates that GA-pretreated, gentamicin-post-fixed bovine pericardium may be used as an alternative biological dressing in the case of large wounds.
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PMID:Use of glutaraldehyde-gentamicin-treated bovine pericardium as a wound dressing. 816 62

A way of fragmentation of Clostridium botulinum neurotoxin was carried out to elucidate the structure-function relationship of neurotoxin. The hitherto only plausible fragment was isolated from the trypsin-treated heavy chain of botulinum type E neurotoxin. In the presence of 4 M urea, one protein peak emerged from QAE-Sephadex column loaded with the heavy chain mildly treated with trypsin by elution with 0.1 M sodium chloride. Although many protein bands were detected in SDS-PAGE of the treated heavy chain, the eluted protein migrated in a single band to the position of 41,000 Da. The recovery of the 41,000-Da fragment was 28.6%, but with a 2 M urea-containing buffer as eluant, the recovery was less than 12%. The 41,000-Da fragment bound to gangliosides GD1a, GT1b, and GQ1b, to which neurotoxin and the heavy chain bound. The 41,000-Da fragment partially interfered with the binding of 125I-labeled neurotoxin to mouse brain synaptosomes. We have proposed a three-fragment structure (L.H-1.H-2) for botulinum type E neurotoxin. The characters of the 41,000-Da fragment described in this paper seem to substantiated our proposal that type E neurotoxin consists of three fragments, L.H-1.H-2, and that the ganglioside-binding fragment is H-2.
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PMID:Purification and characterization of the ganglioside-binding fragment of Clostridium botulinum type E neurotoxin. 842 78

A stable aqueous solution of reduced keratins was prepared by extracting the proteins from wool (Corriedale) with a mixture of urea, mercaptanol, surfactant, and water at 40-60 degrees C. Sodium dodecyl sulfate was especially effective as a surfactant, not only in promoting extraction but also in stabilizing the aqueous protein solution. The proteins had the following constants: MW, 52,000-69,000 daltons; cysteine content, 8-9 mol%; pl about 6.7. A clear film was readily prepared from a keratin solution containing glycerol. The film was insoluble in water and organic solvents including dimethyl sulfoxide. The keratin film was permeable to glucose, urea, and sodium chloride. The keratin film was degraded in vitro (by trypsin) and in vivo (by subcutaneous embedding in mice).
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PMID:Preparation of stable aqueous solution of keratins, and physiochemical and biodegradational properties of films. 883 38

Laboratory investigations were carried out to study the influence of certain medical substances and saline solutions of various concentrations upon activity of trypsin and microbial proteases under similar conditions and regimens of action. Based on the results obtained with regard for the inhibiting effect of medicamentous substances and concentrations of saline solutions upon trypsin and microbial proteases the authors made up a prescription of the saline solution with unithiol, sodium thiosulphate, calcium chloride, sodium chloride. This composition is optimal for the elimination of microbial toxicosis in the injury focus, and facilitates natural development of the wound process.
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PMID:[The effect of different concentrations of saline solutions on the proteolytic activity of trypsin and microbial proteases]. 912 55

In this study, we examined the effects of selected environmental factors on the adhesion of Porphyromonas gingivalis fimbriae, an important structure involved in attachment of the bacteria to human gingival cells. The human gingival carcinoma cell line Ca9-22 was grown in microculture plates, and adherence was detected by use of 125I-labeled fimbriae. Adhesion was increased by changes in pH from 7.0-8.0, but was decreased by increase in the sodium chloride concentration above 0.15 M. Trypsin treatment of Ca9-22 cells also augmented adhesion of the fimbriae to the cells. These results indicate that fimbrial adhesion to gingival cells is controlled by various environmental factors, and the data on trypsin treatment suggest that elevated levels of protease in the gingival sulcus, such as can occur with poor oral hygiene and gingivitis, may expose adhesion molecules on the gingival cell surface, thereby promoting the attachment of P. gingivalis fimbriae.
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PMID:Adhesion of Porphyromonas gingivalis fimbriae to human gingival cell line Ca9-22. 946 73


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