25 The Structure of the Collagen Fibril

Ra, Grant

doi:10.1097/00003086-196911000-00026

Cited by 9 publications

(3 citation statements)

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“…Common to all of these models is an overlap and hole region in each unit cell of total length d (d = 670 A) along the fibril, that would be expected to lead to a step-function in the electron density profile along the unit cell. This type of structure is apparently revealed in negative staining of fibrils where the overlap region, agreeing with the various models, has a length of 0.4 d (13). It has been claimed however, that the overlap region may be as much as 0.6 d (14).…”

Section: Introductionsupporting

confidence: 73%

Experimental confirmation of calculated phases and electron density profile for wet native collagen

Stinson¹,

Bartlett²,

Kurg³

et al. 1979

Biophysical Journal

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An experimental procedure is developed to phase the reflections obtained in x-ray diffraction investigations of collagen in native wet tendons. Phosphotungstic acid was used for isomorphous addition in phase determination and was located by electron microscopy. Structure factors (with phases) were obtained from the electron microscopy data for the heavy metal. Structure-factor magnitudes for collagen with and without the heavy metal were obtained from the x-ray diffraction data. The first 10 orders were investigated. Standard Argand diagrams provided two solutions for each of these, except the weak sixth order. In each case, one of the two possible solutions agrees well with the phases proposed on theoretical grounds by Hulmes et al. The present results suggest that their other proposed phases are probably correct. An electron density profile along the unit cell of the fibril is presented that shows a distinct step, as expected on the basis of the hole-overlap model. The overlap region is 48% of the length of the unit cell.

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Section: Introductionsupporting

confidence: 73%

Experimental confirmation of calculated phases and electron density profile for wet native collagen

Stinson¹,

Bartlett²,

Kurg³

et al. 1979

Biophysical Journal

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“…9) . These fibrils exceed in diameter the typical collagen fibril found in skin or tendon, (Cox and Grant, 1969 ;Grant, Cox, and Horne, 1965), and were observed in aggregates measuring up to 2000 A in diameter. These findings lead to the conclusion that there is a paucity in the mutant matrix of those substances, particularly AMPS, which are deemed responsible for the appearance of normal cartilage matrix .…”

Section: Summary Of Observationsmentioning

confidence: 85%

A New Chondrodystrophic Mutant in Mice

Seegmiller

Fraser

Sheldon

1971

The Journal of Cell Biology

153

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The occurrence of a new mutation affecting cartilage and bone in mice is reported . The gene is lethal, shows autosomal recessive inheritance, and has high penetrance. It is not allelic to shorthead and probably not to phocomelia or achondroplasia . It results in a foreshortened face, cleft palate, defective trachea, and shortened long bones with flared metaphyses . Chondrocytes of epiphyseal cartilage from the mutant are not aligned in columns, and there is a decrease in the usual staining of the cartilage matrix . Electron microscope observations show large, wide collagen fibrils with "native" banding in the matrix of mutant cartilage, which are not present in normal cartilage . Possible explanations for the expression of this genetic disorder of cartilage development are put forward .

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“…20 In relation to glutaraldehyde itself, fixation produces a change in pattern with negative staining (potassium phosphotungstate) which is not altered by deamination or acetylation of the episilon amino group of lysine. 21 It was concluded that the staining changes were due to the bonds themselves and not a charge change from neutralization of the lysine epsilon amino groups. It is felt that glutaraldehyde forms a bridge between two adjacent reactive residues.…”

Section: Discussionmentioning

confidence: 99%

Tendon grafting with glutaraldehyde fixed material

McMaster

Kouzelos

Liddle

et al. 1976

J. Biomed. Mater. Res.

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An evaluation of 0.2% buffered glutaraldehyde fixed tendon as a potential tendon replacement prosthesis was evaluated in rabbit and chicken models. In vivo implantations were done to determine compatability, function, and strength of grafts. Autogenous fresh grafts were used as controls in the strength evaluations. The fixed tendon elicits no cellular rejection response, is invaded and replaced by host tissues, and anastomosis strength in tension compares favorably to a fresh autogenous control. These preliminary evaluations indicate a useful potential for this fixed biomaterial as a tendon prosthesis.

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25 The Structure of the Collagen Fibril

Cited by 9 publications

References 0 publications

Experimental confirmation of calculated phases and electron density profile for wet native collagen

Experimental confirmation of calculated phases and electron density profile for wet native collagen

A New Chondrodystrophic Mutant in Mice

Tendon grafting with glutaraldehyde fixed material

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