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Extraction of bovine vitreous collagens and characterisation of their forms in vivo.

Paul Nicholas Bishop

Extraction of bovine vitreous collagens and characterisation of their forms in vivo.

by Paul Nicholas Bishop

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Published by University of Manchester in Manchester .
Written in English


Edition Notes

Thesis (Ph.D.), - University of Manchester, School of Biological Sciences.

ContributionsUniversity of Manchester. School of Biological Sciences.
The Physical Object
Pagination205p.
Number of Pages205
ID Numbers
Open LibraryOL16573392M

We were able to separate pepsin-solubilized collagen of the bovine vitreous body into three distinct fractions by differential salt precipitation with M acetic acid containing M, M, and M NaCl, respectively. The M NaCl fraction showed (1) an electrophoretic mobility in polyacrylamide gel identical to that of type II collagen, (2) CNBr-derived peptides very similar to type.   Bovine vitreous gel was solubilized (apart from a residual collagenous pellet) in 4 M guanidine hydrochloride and after dialysis into phosphate buffered saline analyzed by gel filtration chromatography with in-line measurement of refractive index and multi-angle laser light scattering. Characterization of their forms in vivo. Ayad S.

vitreous was either used directly or a disc-like section was cut with the axis of the disc coinciding with the anterior-to-posterior axis of the eye (typically – g). Some of the vitreous discs were loaded into a cleated 25 mm parallel disc geometry for mechanical characterization, and the remainder were used for network stability studies. Collagens and non collagenous proteins in the human eye. I. Corneal stroma in vivo and keratocyte production in vitro. Current Eye Research , 1 (2), DOI: / Jack N. Liang, Bireswar Chakrabarti. Spectroscopic studies on pepsin-solubilized vitreous and cartilage collagens.

Comparisons of the artheritogenic and immunologic properties of collagens from bovine articular cartilage (type II) and vitreous showed that the two were indistinguishable by . The distance between collagen fibrils in the rabbit vitreous has been studied by freeze-cleavage replica techniques (Pajor, ). The interfibril distance was found to be – µLm, which approximated estimates for the bovine vitreous (Balazs, ) and measurements in the albino rat (Hansson, ).


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Extraction of bovine vitreous collagens and characterisation of their forms in vivo by Paul Nicholas Bishop Download PDF EPUB FB2

Ayad S, Marriott A, Morgan K, Grant ME. Bovine cartilage types VI and IX collagens. Characterization of their forms in vivo.

Biochem J. Sep 15; (3)– [PMC free article] Ayad S, Marriott A, Brierley VH, Grant ME. Mammalian cartilage synthesizes both proteoglycan and non-proteoglycan forms of type IX by:   Isolation from bovine elastic tissues of collagen type VI and characterization of its form in vivo.

Biochem J. Sep 1; (2)– [PMC free article] Ayad S, Kwan AP, Grant ME. Partial characterization of type X collagen from bovine growth-plate cartilage.

Evidence that type X collagen is processed in vivo. FEBS by:   Ayad S, Chambers CA, Shuttleworth CA, Grant ME. Isolation from bovine elastic tissues of collagen type VI and characterization of its form in vivo. Biochem J. Sep 1; (2)– [PMC free article] [Google Scholar] Ayad S, Kwan AP, Grant ME.

Partial characterization of type X collagen from bovine growth-plate by:   We provide the first biochemical characterisation of intact type IX collagen extracted from bovine vitreous. It possesses a shortened α1(IX) chain (M r 64K) compared to its cartilage counterpart (M r 84K).

All the vitreous type IX collagen is in a proteoglycan form, its glycosaminoglycan constituent being a chondroitin/dermatan sulphate component of M r 15–60K attached to the α2(IX) Cited by:   To date, a significant amount of work has been dedicated to the study of the anatomical and physiological structure of the vitreous.

Amongst which, there have been few studies that have investigated diffusion through the vitreous humours, typically using ex vivo animal vitreous.

For instance, Käsdorf et al. () have studied FITC-dextran and peptide penetration into the ovine vitreous Cited by: 7. S Ayad's 60 research works with 2, citations and 1, reads, including: The expression of types X and VI collagen and fibrillin in rat mandibular condylar cartilage Response to mastication forces.

Acknowledgements PNB is a Wellcome Trust Clinician Scientist Fellow. The authors would also like to thank the Guide Dogs for the Blind Association for their support. Vitreous Versican and Hyaluronan References Ayad, S., Marriot, A., Morgan, K.

and Grant, M.E.: Bovine cartilage types VI and IX collagens. Characterization of their forms in vivo. • Background. Heterotypic (mixed) collagen fibrils that contain collagen types II, IX and V/XI have previously been identified in vitreous gel.

The purpose of this study was to determine whether vitreous gel also contains type VI collagen microfibrils, as they are widely distributed in other tissues where they may play an important structural role. • Methods. Bovine and human vitreous gel.

Bovine vitreous-humour collagen alpha-chains differed, however, from those of cartilage collagen in that they had a lower alanine content and differed in their susceptibility to cleavage by CNBr.

Satisfactory cleavage was obtained after two CNBr treatments involving reduction and alkylation. in the free form, however. Some is bound to proteins and glycosaminoglycans. The bound water is between 15% and 20% of all water content (the rest being free water), as measured in monkey and bovine vitreous, respectively.5,32 1.

Proteins The protein content of the vitreous, although small as a percentage of the overall content, is. Isolation and native characterization of cysteine-rich collagens from bovine placental tissues and uterus and their relationship to types IV and V collagens.

Biosci Rep. Jul; 2 (7)– Ayad S, Abedin MZ, Grundy SM, Weiss JB. Isolation and characterisation of an unusual collagen from hyaline cartilage and intervertebral disc.

Bishop PN, Crossman MV, McLeod D, Ayad S. Extraction and characterisation of the tissue forms of collagen types II and IX from bovine vitreous. Biochem J ; – CAS; Article. «hide 10 20 30 40 50 mapaadprsl lvllqvlgla laqirglpge pgppgppgpp gvpgsdgidg 60 70 80 90 dkgppgkagp pgpkgepgka gtdgpdgkpg idgltgakge pgpagipgvk gqpglpgppg lpgpgfagpp gppgpvglpg eigltgpkgd pgpegpsgpp gppgkpgrpg tiqglegsad flcptncpag vkgppglqgv kghpgrrgll gdsgrqgkpg pkgdvgasge qgipgppgpq gvrgypgmag.

Most collagens are able to form supramolecular aggregates. Besides triple-helical domains, collagens contain non-triple-helical (NC) domains, used as building blocks by other ECM proteins. The molecular structure and supramolecular assembly of collagens allow their division into major subfamilies, depending on the supramolecular structure such.

We report for the first time that, after centrifugation of adult bovine vitreous, the hyaluronan-rich supernatant contains collagens which can be isolated in their intact forms by precipitation.

Wang L, An X, Yang F, Xin Z, Zhao L, et al. Isolation and characterisation of collagens from the skin, scale and bone of deep-sea red sh (Sebastes mentella). Food Chemistry. ; Isolation and Characterisation of Major and Minor Collagens from Hyaline Cartilage of Hoki (Macruronus novaezelandiae) Article (PDF Available) in Marine Drugs.

Collagens are the most abundant high molecular weight proteins in both invertebrate and vertebrate organisms, including mammals, and possess mainly a structural role, existing different types according with their specific organization in distinct tissues. From this, they have been elected as one of the key biological materials in tissue regeneration approaches.

Then, washings with cold distilled water are performed until the pH stabilizes at The use of a 10% solution of sodium chloride (NaCl) at (w/v) sample-to-solvent ratio has been also.

Both isoforms have also been detected in the embryonic and adult canine retina (Du et al., ), as well as in fetal and adult bovine vitreous with the type IIA form predominating (Bishop et al., ).

In the mouse eye, synthesis of types IIA and IIB mRNA transcripts has been detected during embryogenesis starting at least from embryonic day. This has been exploited for purification. Types I and III collagen in 2 M guanidine-HCl, pH solution can be denatured and the constituent chains separate in solution.

Dialysis against deionized water, to remove the guanidine, allows the denatured collagens to refold into their triple-helical structures, and to form .Miller EJ, Gay S. The collagens: an overview and update. Methods Enzymol. ; – Bishop PN, Crossman MV, McLeod D, Ayad S.

Extraction and characterization of the tissue forms of collagen types II and IX from bovine vitreous. Biochem J. Apr 15; (Pt 2)– [PMC free article]. Isolation and characterization of papain solubilized collagen from bovine spinous process cartilage.

International Journal of Biochemistry8 (5), DOI: /X(77)X. Edward J. Miller. Biochemical characteristics and biological significance of the genetically-distinct collagens.