Effect of Glutaraldehyde on Properties of Membranes Prepared from Fish Scale Collagen

2012 ◽  
Vol 1418 ◽  
Author(s):  
Zhefeng Xu ◽  
Toshiyuki Ikoma ◽  
Tomohiko Yoshioka ◽  
Motohiro Tagaya ◽  
Satoshi Motozuka ◽  
...  

ABSTRACTCollagen fibril membranes (CFMs) with a high mechanical property were fabricated with a lateral face evaporation method, in which type I atelocollagen extracted from tilapia scales was used. The density and thickness of the CFM obtained were 0.51 ± 0.04 mg/cm3 and 50 ± 5 μm. The collagen fibrils in the CFM had a similar periodic stripped pattern of 67 nm with native collagen fibrils. The CFM was crosslinked in gaseous glutaraldehyde for different duration in order to increase the mechanical property. The crosslinking degrees of the CFMs analyzed by free amino groups gradually increased to 70.3 % against the exposure duration until 6 hours, and reached a plateau. The denaturation temperatures of the CFMs with the crosslinking degrees at 20.4 % to 43% were linearly increased from 49°C to 75°C. The tensile strength of the CFMs was slightly improved until the crosslinking degree at 33.3 % and then the tensile strength rapidly increased to be 68 MPa. It was suggested that a percolation phenomenon took place in the CFMs by crosslinking of collagen fibrils with polymerized GA molecules.

Materials ◽  
2020 ◽  
Vol 13 (2) ◽  
pp. 358 ◽  
Author(s):  
Haiyan Ju ◽  
Xiuying Liu ◽  
Gang Zhang ◽  
Dezheng Liu ◽  
Yongsheng Yang

Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.


2014 ◽  
Vol 1035 ◽  
pp. 303-306
Author(s):  
Xiao Ya Chen ◽  
Quan An Li ◽  
Qing Zhang ◽  
Jun Chen ◽  
Hui Zhen Jiang

The microstructure and mechanical properties of Mg-6Al-1Zn-0.9Y-1.8Gd alloy have been studied by micro-analysis and tensile tests. The results showed that the alloy mainly consists of Mg matrix, Al2Y, Mg17Al12and Al2Gd. The best tensile strength of the alloy was 255 Mpa at room temperature, and the alloy still had the very high mechanical property at high temperature.


1988 ◽  
Vol 36 (11) ◽  
pp. 1425-1432 ◽  
Author(s):  
R Fleischmajer ◽  
J S Perlish ◽  
R Timpl ◽  
B R Olsen

The purpose of this study was to correlate ultrastructural features of tendon collagen fibrils at various stages of development with the presence of procollagen, pN-collagen, pC-collagen, and the free amino propeptides and carboxyl propeptide of type I procollagen. Tendons from 10-, 14-, and 18-day chicken embryos reveal small, well-defined intercellular compartments containing collagen fibrils with diameters showing a unimodal distribution. At 21 days (hatching) and 9 days (post hatching) and at 5 weeks (post hatching), the compartments are larger, less well-defined, and there is multimodal distribution of tendon fibril diameters. Procollagen and the intermediates pN-collagen and pC-collagen are present in tendons up to 18 days. Thereafter there is a marked reduction in procollagen, whereas the intermediates persist throughout all stages of development. Similarly, free amino propeptides and carboxyl propeptides of type I procollagen were found at all stages. The amino propeptide of type III procollagen was restricted to the peritendineum until 7 weeks post hatching. At that time, a network of fibrils containing the amino propeptide of type III procollagen was seen delineating well-circumscribed compartments of collagen fibrils throughout the entire tendon. This study supports the notion that pN- and pC-collagen have an extracellular role and participate in collagen fibrillogenesis.


Micron ◽  
2009 ◽  
Vol 40 (5-6) ◽  
pp. 665-668 ◽  
Author(s):  
Mitsuhiro Okuda ◽  
Masaki Takeguchi ◽  
Motohiro Tagaya ◽  
Toru Tonegawa ◽  
Ayako Hashimoto ◽  
...  

Author(s):  
C. N. Sun ◽  
H. J. White

Previously, we have reported on extracellular cross-striated banded structures in human connective tissues of a variety of organs (1). Since then, more material has been examined and other techniques applied. Recently, we studied a fibrocytic meningioma of the falx. After the specimen was fixed in 4% buffered glutaraldehyde and post-fixed in 1% buffered osmium tetroxide, other routine procedures were followed for embedding in Epon 812. Sections were stained with uranyl acetate and lead citrate. There were numerous cross striated banded structures in aggregated bundle forms found in the connecfive tissue of the tumor. The banded material has a periodicity of about 450 Å and where it assumes a filamentous arrangement, appears to be about 800 Å in diameter. In comparison with the vicinal native collagen fibrils, the banded material Is sometimes about twice the diameter of native collagen.


1963 ◽  
Vol 42 (2) ◽  
pp. 209-213 ◽  
Author(s):  
Arthur I. Cohen ◽  
Edward H. Frieden

ABSTRACT A number of corticotrophin analogues have been prepared, some of which potentiate the biological activity of the untreated hormone in vitro. The free amino groups of corticotrophin appear to be essential not only for hormonal activity, but also for the interaction of the analogues with the tissue corticotrophin inactivating system which is assumed to account for the potentiating effect.


Diabetes ◽  
1985 ◽  
Vol 34 (8) ◽  
pp. 812-815 ◽  
Author(s):  
L. Borghi ◽  
R. Lugari ◽  
A. Montanari ◽  
P. Dall'Argine ◽  
G. F. Elia ◽  
...  

1955 ◽  
Vol 216 (2) ◽  
pp. 621-624
Author(s):  
Mary L. McFadden ◽  
Emil L. Smith

1955 ◽  
Vol 214 (1) ◽  
pp. 185-196 ◽  
Author(s):  
Mary L. McFadden ◽  
Emil L. Smith

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