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1.
Bull Exp Biol Med ; 174(4): 514-517, 2023 Feb.
Article in English | MEDLINE | ID: mdl-36913093

ABSTRACT

We performed a comprehensive assessment of the acellular dermal matrix obtained during the detergent-enzymatic treatment of the porcine dermis. Acellular dermal matrix was used for the experimental treatment of a hernial defect in a pig using the sublay method. Sixty days after the surgery, biopsy specimens were obtained from the area of hernia repair. The acellular dermal matrix can be easily modeled depending on the size and shape of the defect during surgical procedures, can eliminate the defect of the anterior abdominal wall, and is resistant to cutting by the suture material. Histological examination demonstrated replacement of the acellular dermal matrix with newly formed connective tissue.


Subject(s)
Abdominal Wall , Acellular Dermis , Plastic Surgery Procedures , Animals , Swine , Herniorrhaphy , Abdominal Wall/surgery
2.
Bull Exp Biol Med ; 170(3): 378-383, 2021 Jan.
Article in English | MEDLINE | ID: mdl-33452991

ABSTRACT

The tissue reaction of pig skin to implantation of decellularized and recellularized dermal matrices on a formed wound defect was evaluated by histological methods on days 2, 5, 8, 16, and 20 after surgery. Differences in tissue response to different matrices were identified. In experimental wounds coated with decellularized dermal matrices, we observed the formation of a scar tissue, which required autodermoplasty on day 12 of the experiment. In wounds coated with recellularized dermal matrices, all layers of the skin completely recovered by day 20 after surgery with the formation of full dermal and epidermal layers. Our findings suggest that reparative morphological changes in the wound depend on the presence of fibroblasts in the implanted dermal matrix.


Subject(s)
Skin/cytology , Tissue Engineering/methods , Tissue Scaffolds/chemistry , Animals , Extracellular Matrix , Fibroblasts/cytology , Swine , Wound Healing/physiology
3.
Bull Exp Biol Med ; 162(5): 703-706, 2017 Mar.
Article in English | MEDLINE | ID: mdl-28361431

ABSTRACT

We modified the protocol of obtaining of biological scaffolds of rat lungs based on dynamic recording of specific resistivity of working detergent solution (conductometry) during perfusion decellularization. Termination of sodium deoxycholate exposure after attaining ionic equilibrium plateau did not impair the quality of decellularization and preserved structural matrix components, which was confirmed by morphological analysis and quantitative assay of residual DNA.


Subject(s)
Lung , Tissue Scaffolds , Animals , Conductometry , Deoxycholic Acid/chemistry , Detergents/chemistry , Electric Conductivity , Lung/cytology , Male , Rats, Wistar , Solutions , Tissue Engineering , Tissue Fixation
4.
Prikl Biokhim Mikrobiol ; 42(6): 638-44, 2006.
Article in Russian | MEDLINE | ID: mdl-17168292

ABSTRACT

Twenty strains of the wood-degrading fungi from the genus Trametes Fr., capable of synthesizing laccases, were screened according to the changes in the oxidase activity in a submerged culture. The range of maximal efficiency of various species with respect to extracellular oxidase activity was determined. The absence of correlation between the oxidase activity in a submerged culture and the size of colored zone on agar media (Bavendamm reaction) was demonstrated. The most efficient strains, T. hirsita 56 and T. ochracea 92-78, were used to produce laccases, homogeneous according to SDS electrophoresis data. A number of biochemical parameters characteristic of these enzymes were determined.


Subject(s)
Fungal Proteins/analysis , Fungal Proteins/biosynthesis , Laccase/analysis , Laccase/biosynthesis , Polyporales/enzymology , Basidiomycota/enzymology , Basidiomycota/growth & development , Cell Culture Techniques , Oxidoreductases/analysis , Oxidoreductases/biosynthesis , Polyporales/growth & development
5.
Biochemistry (Mosc) ; 70(11): 1274-9, 2005 Nov.
Article in English | MEDLINE | ID: mdl-16336189

ABSTRACT

A method for purification of enzymes from the ligninolityc complex of the basidiomycete Trametes pubescens (Schumach.) Pilat has been elaborated. Two homogeneous isoforms of laccases (laccase 1 and laccase 2) as well as a homogeneous preparation of lignin peroxidase were isolated. Basic biochemical parameters of the enzymes were determined, such as the molecular weights (67, 67, and 45 kD, respectively), isoelectric points (5.3, 5.1, and 4.2, respectively), as well as content and composition of the carbohydrate moiety of the laccases (N-acetylglucosamine, mannose, and xylose). The pH dependences and thermal stabilities of the laccases were investigated. The kinetic parameters of the enzymatic reactions catalyzed by the laccases were determined using different substrates, such as catechol, hydroquinone, 2,2 -azinobis-(3-ethylbenzthiazoline-6-sulfonate), and K4Fe(CN)6. The structure of the active sites of both laccases and the lignin peroxidase were studied by EPR, CD, and UV-VIS spectroscopy, as well as using fluorescence analysis. Our studies showed similarity of the spectral characteristics of the two laccases, whereas their kinetic properties were found to be different.


Subject(s)
Basidiomycota/enzymology , Laccase/isolation & purification , Lignin/metabolism , Peroxidases/isolation & purification , Chromatography, Liquid , Circular Dichroism , Electron Spin Resonance Spectroscopy , Electrophoresis, Polyacrylamide Gel , Hydrolysis , Laccase/metabolism , Peroxidases/metabolism , Spectrometry, Fluorescence , Spectrophotometry, Ultraviolet
6.
Biochimie ; 86(9-10): 693-703, 2004.
Article in English | MEDLINE | ID: mdl-15556280

ABSTRACT

New strains of basidiomycetes producing extracellular laccases (Trametes ochracea 92-78, and Trametes hirsuta 56) have been found by screening of isolates of Trametes fungi. The laccases from T. hirsuta 56 and T. ochracea 92-78 as well as two laccases from previously found and described strains of basidiomycetes, namely Cerrena maxima and Coriolopsis fulvocinerea, were purified to homogeneity. The standard redox potentials of type 1 copper in the enzymes were determined and found to be 780, 790, 750, and 780 mV, respectively. The spectral and biochemical studies showed that the enzymes had no significant differences between the structures of their active sites (T1, T2, and T3). In spite of this fact, the basic biochemical properties as well as the redox potentials of the T1 sites of the enzymes were found to be different. The molecular weights of the laccases range from 64 to 70 kDa, and their pI values range from 3.5 to 4.7. The pH-optima are in the range 3.5-5.2. The temperature optimum for activity is about 50 degrees C. The thermal stabilities of the enzymes were studied. The catalytic and Michaelis constants for catechol, guaiacol, hydroquinone, sinapinic acid, and K(4)Fe(CN)(6) were determined. Based on these results as well as results obtained by comparing with published properties of several laccases, it could be concluded that T. hirsuta and Cerrena maxima laccases have some superior characteristics such as high stability, high activity, and low carbohydrate content, making them attractive objects for further investigations as well as for application in different areas of biotechnology.


Subject(s)
Basidiomycota/enzymology , Fungal Proteins/chemistry , Laccase/chemistry , Binding Sites , Substrate Specificity
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