ABSTRACT
The authors report surgical treatment of a patient with a penetrating abdominal trauma followed by damage to inferior vena cava, liver, duodenum and pancreas, massive bleeding and large retroperitoneal hematoma. Suturing of inferior vena cava defect, liver and pancreas, Billroth II gastric resection, drainage of retroperitoneal space and abdominal cavity were carried out. Postoperative period was complicated by pneumonia and seroma in lesser sac that required percutaneous puncture. Antibiotic therapy was used postoperatively. The patient was discharged in 25 days after surgery.
Subject(s)
Abdominal Injuries , Wounds, Penetrating , Abdominal Injuries/complications , Abdominal Injuries/diagnosis , Abdominal Injuries/surgery , Humans , Liver/injuries , Retroperitoneal Space , Vena Cava, Inferior/diagnostic imaging , Vena Cava, Inferior/injuries , Vena Cava, Inferior/surgeryABSTRACT
The chitin-binding ability of isoperoxidases isolated from 23 plants of different species was studied. The activation of peroxidases in a protein extract in the presence of this polysaccharide was found for 14 of the studied plants. Anionic isoperoxidases were shown to be sorbed on chitin and eluted from them with 1 M NaCl for 16 of the plant species. Cationic isoforms of the peroxidases of some species of the Fabaceae and Cucurbitaceae plant families also bound to chitin. An immunochemical similarity was found between the chitin-binding isoperoxidases of taxonomically distant plant species (the Pomaceous, Fabaceae, and gourd families). Moreover, a high homology of the molecular structures of the polysaccharide-binding sites was revealed for the anionic peroxidases of rice, wheat, oat, zucchini, cucumber, and radish. We propose the existence of a special class of plant peroxidases that bind with polysaccharides (chitin) and participate in the protective reactions of plants against pathogens.
Subject(s)
Chitin/chemistry , Peroxidases/chemistry , Plant Proteins/chemistry , Enzyme Activation , Immunoassay , Isoelectric Focusing , Isoenzymes/chemistry , Phylogeny , Protein BindingSubject(s)
Antineoplastic Agents/pharmacology , Melanoma, Experimental/drug therapy , Soybean Proteins/pharmacology , Animals , Antineoplastic Agents/administration & dosage , Cyclophosphamide/pharmacology , Female , Mice , Mice, Inbred C57BL , Soybean Proteins/administration & dosage , Tegafur/pharmacologyABSTRACT
The specificity of the peptide hydrolyzing action of a highly purified preparation of kininase from Latrodectus Tredecimguttatus venom was studied by the method of TLC on silica gel with the use of various synthetic peptides as substrates. It was shown that the enzyme cleaves the -Pro(7)-Phe(8)-bonds in BK and AI molecules liberating, correspondingly, the C-terminal dipeptide and tripeptide. Exopeptidase specificity was not revealed in the enzyme activity with the use of a number of free and N-substituted tri- and pentapeptides. The results obtained characterize the spider venom kininase as a thiol endopeptidase, which cleaves internal peptide bonds at the proline carboxyl end.
Subject(s)
Endopeptidases/analysis , Kinins/metabolism , Spider Venoms/enzymology , Angiotensin II/metabolism , Animals , Bradykinin/metabolism , Chromatography, Thin Layer , Peptidyl-Dipeptidase A/analysis , Substrate SpecificityABSTRACT
The nature of the bradykinin (BK)-hydrolyzing (kininase) activity of peptidhydrolase isolated from spider (Latr. tredecimguttatus) venom has been studied. It was found that the BKase activity of the enzyme is fully inhibited by organic mercurials (10(-5)-10(-6) M) as well as by 5,5'-dithiobis(2-nitrobenzoic acid) (10(-7) M); the latter blocks three SH-groups within the enzyme molecule. Serine and metalloproteinase inhibitors have no effect on the kininase activity. Thin-layer chromatography on silicagel revealed that the highly purified enzyme hydrolyzes the -Pro7-Phe8- bond of BK liberating the C-terminal dipeptide, HPhe-ArgOH. Besides, the kininase splits off the C-terminal tripeptide from angiotensin I by hydrolyzing its -Pro7-Phe8-bond. The enzyme does not exhibit any exopeptidase activity with free and N-substituted tri- and pentapeptides. The data obtained suggest that the Latr. tredecimguttatus kininase can be related to thiol endopeptidases hydrolyzing the peptide bonds formed by proline carboxyl.
Subject(s)
Bradykinin/metabolism , Endopeptidases , Lysine Carboxypeptidase/isolation & purification , Spider Venoms/chemistry , Sulfhydryl Compounds/metabolism , Amino Acid Sequence , Binding Sites , Catalysis , Chromatography, Thin Layer , Hydrolysis , Lysine Carboxypeptidase/antagonists & inhibitors , Lysine Carboxypeptidase/metabolism , Molecular Sequence Data , Protease Inhibitors , Substrate SpecificityABSTRACT
Two vasoactive peptides are isolated from the Vespa orientalis venom by gel filtration and ion-exchange chromatography. The physicochemical and functional properties of peptides are studied. Vasoactive peptides show the myotropic activity and hypotensive action which is of prolonged character as compared with bradykinin. Their complete amino acidic sequences are determined. One of the peptides is a similar structural analogue of bradykinin.
Subject(s)
Bee Venoms/analysis , Peptides/isolation & purification , Vasomotor System/drug effects , Wasp Venoms/analysis , Amino Acid Sequence , Animals , Blood Pressure/drug effects , Bradykinin/pharmacology , Cats , Chromatography, Thin Layer , Isoelectric Focusing , Molecular Sequence Data , Peptides/pharmacologySubject(s)
Angiotensin-Converting Enzyme Inhibitors , Bradykinin/pharmacology , Peptides/pharmacology , Peptidyl-Dipeptidase A , Spider Venoms/antagonists & inhibitors , Spiders , Amino Acids/analysis , Animals , Cattle , Chemical Phenomena , Chemistry, Physical , Drug Synergism , Female , Kidney/enzymology , Peptides/analysis , Peptides/isolation & purification , Rats , Spider Venoms/analysis , Uterine Contraction/drug effectsSubject(s)
Arthropod Venoms/analysis , Cysteine Endopeptidases/isolation & purification , Spider Venoms/analysis , Animals , Blood Pressure/drug effects , Bradykinin/metabolism , Cats , Chromatography, DEAE-Cellulose , Chromatography, Gel , Cysteine Endopeptidases/metabolism , Cysteine Endopeptidases/pharmacology , Kinetics , Protease Inhibitors/pharmacologySubject(s)
Bee Venoms/analysis , Peptides/isolation & purification , Wasp Venoms/analysis , Amino Acid Sequence , Animals , Biological Assay , Cardiovascular Agents , Chromatography, Gel , Female , Histamine Release/drug effects , In Vitro Techniques , Molecular Sequence Data , Peptides/pharmacology , Rats , Uterine Contraction/drug effectsSubject(s)
Arthropod Venoms/pharmacology , Bradykinin/metabolism , Peptide Hydrolases/pharmacology , Peptidyl-Dipeptidase A/pharmacology , Spider Venoms/pharmacology , Amino Acids/analysis , Animals , Bradykinin/antagonists & inhibitors , Catalysis , Chemical Phenomena , Chemistry, Physical , Hydrogen-Ion Concentration , Kinetics , Molecular Weight , Peptide Hydrolases/analysis , Peptide Hydrolases/isolation & purification , Peptidyl-Dipeptidase A/analysis , Peptidyl-Dipeptidase A/isolation & purification , Spider Venoms/analysis , Spider Venoms/isolation & purificationSubject(s)
Arthropod Venoms/analysis , Cholinesterase Inhibitors/pharmacology , Cholinesterases/isolation & purification , Spider Venoms/analysis , Spiders/enzymology , Acetylcholinesterase/analysis , Acetylcholinesterase/isolation & purification , Animals , Cholinesterases/analysis , Scorpion Venoms/analysis , Scorpions/enzymology , Substrate Specificity/drug effectsSubject(s)
Arthropod Venoms/pharmacology , Mitochondria, Liver/drug effects , Spider Venoms/pharmacology , Animals , Dose-Response Relationship, Drug , In Vitro Techniques , Male , Mitochondria, Liver/metabolism , Mitochondrial Swelling/drug effects , Oxidative Phosphorylation/drug effects , Oxygen Consumption/drug effects , Phospholipases A/metabolism , RatsABSTRACT
In a chronic experiment dogs were exposed to irradiation in doses of 190, 360 and 560 rad for 3 years. As compared to the unirradiated controls they showed a slower recovery of the albumin and cholesterol content in the blood. The cholesterol content varied, depending on the dose of chronic irradiation, whereas the protein content did not show such a correlation.
Subject(s)
Blood Proteins/radiation effects , Cholesterol/radiation effects , Radiation Injuries, Experimental/blood , Animals , Cholesterol/blood , Chronic Disease , Dogs , Dose-Response Relationship, Radiation , Gamma Rays/adverse effectsABSTRACT
The paper presents the results of a many-year investigation of the sugar content in dogs irradiated with total doses of 125, 370, 720, 750, 1130 rad. During the first year the sugar content tended to increase and later to decrease. Irradiated and untreated animals showed different reactions to additional loads (running, thermal exposure, acute irradiation). The differences included the direction and level of changes in the sugar content. There was no correlation between the changes and the dose rate. The changes returned to normal after termination of the exposure.