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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
1

Weefselcollagenase en zijn substraten Tissue collagenase and its substrates /

Bos, Teunis van den, January 1979 (has links)
Thesis (doctoral)--Utrecht, 1979.
2

Production of Collagenase Inhibitor by Mouse Calvaria in Tissue Culture

SAKAMOTO, SEIZABURO, NAGAYAMA, MASARU 11 1900 (has links)
No description available.
3

Tissue inhibitor of metalloproteinase-1 expression by human hepatic lipocytes and its role in liver disease

Iredale, John Peter January 1994 (has links)
No description available.
4

Collagenolytic activities of intercranial tumours : In-vitro biochemical and immunolocalization studies

Halaka, A. N. A. M. January 1986 (has links)
No description available.
5

Identification and Targeting of Collagen in the Capsule of Rat Knees with Immobilization-Induced Flexion Contractures

Wong, Kayleigh January 2015 (has links)
Immobility causes joint contractures, loss in range of motion (ROM), notably in elderly and bed-ridden patients. In a rat knee immobilization flexion contracture (FC) model, the posterior capsule contributes to irreversible limitation of ROM. Through microarray, extracellular matrix and collagen pathways were identified as differentially expressed in the posterior capsule of knees with FC. We hypothesized that intra-articular injection of collagenases in rats with knee FC will interfere with collagen in the capsule and allow increased ROM. After four weeks of hind-limb immobilization, rats develop knee FC; two weeks of remobilization with collagenase treatment showed increased ROM compared to buffer injected knees of 8.043° (p-value=0.046). Histological analysis of knee sections revealed changes in collagen content of the extracellular matrix in posterior capsule. In vitro incubation of rat capsules with collagenases confirmed changes in collagen. Along with current rehabilitation methods, treatment with collagenase may augment ROM recovery from knee joint contractures.
6

Isolation and Characterization of Mouse Bone Collagenase Inhibitor

SAKAMOTO, SEIZABURO, NAGAYAMA, MASARU 11 1900 (has links)
No description available.
7

Novel roles for matix metalloproteinases in cell-matrix interactions

Messent, Anthea Jane January 1997 (has links)
No description available.
8

Bioactive Chitosan Nanoparticles and Photodynamic Therapy Inhibit Collagen Degradation in vitro

Persadmehr, Anousheh 09 December 2013 (has links)
This study evaluated the ability of photodynamic therapy (PDT), chitosan nanoparticles (CSnp), or their combination, to inhibit bacterial collagenase-mediated degradation of collagen. Rat type 1 fibrillar collagen matrices were untreated or treated with 2.5% glutaraldehyde (GD), 2.5% GD followed by 1% CSnp, 1% CSnp, PDT, or 1% CSnp followed by PDT. Samples, except untreated controls, were exposed to Clostridium histolyticum collagenase. The soluble digestion products were assessed by hydroxyproline assay and the remaining adherent collagen was quantified by picrosirius red (PSR) staining. Collagen treated with CSnp, PDT, or a combination of CSnp and PDT, exhibited less degradation than controls. The abundance of posttreatment residual collagen correlated with the extent of degradation. Fourier transform infrared (FTIR) spectroscopy analysis showed that PDT treatment enhanced collagen cross-linking. Immunoblotting of sedimented CSnp indicated that CSnp and collagenase bound with low affinity. However, CSnp-bound collagenase showed a significant reduction in collagenolytic activity compared with controls.
9

Bioactive Chitosan Nanoparticles and Photodynamic Therapy Inhibit Collagen Degradation in vitro

Persadmehr, Anousheh 09 December 2013 (has links)
This study evaluated the ability of photodynamic therapy (PDT), chitosan nanoparticles (CSnp), or their combination, to inhibit bacterial collagenase-mediated degradation of collagen. Rat type 1 fibrillar collagen matrices were untreated or treated with 2.5% glutaraldehyde (GD), 2.5% GD followed by 1% CSnp, 1% CSnp, PDT, or 1% CSnp followed by PDT. Samples, except untreated controls, were exposed to Clostridium histolyticum collagenase. The soluble digestion products were assessed by hydroxyproline assay and the remaining adherent collagen was quantified by picrosirius red (PSR) staining. Collagen treated with CSnp, PDT, or a combination of CSnp and PDT, exhibited less degradation than controls. The abundance of posttreatment residual collagen correlated with the extent of degradation. Fourier transform infrared (FTIR) spectroscopy analysis showed that PDT treatment enhanced collagen cross-linking. Immunoblotting of sedimented CSnp indicated that CSnp and collagenase bound with low affinity. However, CSnp-bound collagenase showed a significant reduction in collagenolytic activity compared with controls.
10

Studium vybraných modifikovaných kolagenových biomateriálů / Study of some modified colagen biomaterials

Zouharová, Lucie January 2009 (has links)
The aim of the presented work is the study and biochemical characterization of some modified collagen materials (prepared on Institute of Material Science, Faculty of Chemistry, BUT), optimalization of collagen isolation from various types of animal tissues and testing of isolated collagen stability. First, isolation of collagen from five different animal tissues was performed with satisfactory yields. The concentration of total proteins was measured by Biuret and Hartree – Lowry method, the concentration of free amino groups was measured by TNBSA method. Protein analysis in colllagen preparatives was peformed by vertical electrophoresis PAGE-SDS and by microfluidic electrophoretic system Experion for comparison. Further purification and separation of collagen isolates by gel permeation chromatography was tested too. To detailed characterization thermal stability of collagen specimens was performed by high performance ultrasonic spectroscopy. Biological stability of collagen was tested in model physiological conditions.

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