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Metabolic and Genetic Alterations in Early and Exudative Age-Related Macular Degeneration: Inosine, Amino Acids, and <i>COL2A1</i> Gene Variant. [PDF]
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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1986
The major collagen in lamprey notochord is type II, as determined by its amino acid composition and solubility properties. This collagen has a distribution of charged residues indistinguishable from higher vertebrate Type II collagens as judged by its SLS banding pattern.
S B, Sheren +7 more
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The major collagen in lamprey notochord is type II, as determined by its amino acid composition and solubility properties. This collagen has a distribution of charged residues indistinguishable from higher vertebrate Type II collagens as judged by its SLS banding pattern.
S B, Sheren +7 more
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Mechanical property and biocompatibility of silk fibroin-collagen type II composite membrane.
Materials Science and Engineering C: Materials for Biological Applications, 2019Osteoarthritis is caused by injuries and cartilage degeneration. Cartilage tissue engineering provides new ideas for the treatment of osteoarthritis. Herein, the different ratios composite membranes of silk fibroin/collagen type II were constructed (SF50-
Xianglong Lin +5 more
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Radioimmunoassay for Human Type II Collagen
Journal of Immunoassay, 1990Human articular cartilage type II collagen (h coll.II) was purified and used to develop a radioimmunoassay. The sequential saturation procedure allowed a sensitivity of 3 ng/tube. The intra and between assay coefficients of variation were less than 10 and 20% respectively in the linear part of the curve.
Henrotin, Yves +4 more
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Biofactors, 2016
During degeneration process, the catabolism of collagen type II and anabolism of collagen type I in nucleus pulposus (NP) may influence the bioactivity of transplanted cells.
Yiqing Tao +6 more
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During degeneration process, the catabolism of collagen type II and anabolism of collagen type I in nucleus pulposus (NP) may influence the bioactivity of transplanted cells.
Yiqing Tao +6 more
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Structure of the Type II Collagen Genea
Annals of the New York Academy of Sciences, 1985In summary, the exon/intron structure of the chicken type II collagen gene is identical with that of the chicken alpha 2(I) collagen gene and differs at only one known position from the human and mouse alpha 1(I) genes. However, the chicken type II gene is different from the chicken alpha 2(I) gene in that it is considerably shorter because of a much ...
W B, Upholt, C M, Strom, L J, Sandell
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Characteristics of cellular immune responses to collagen type I or collagen type II
Cellular Immunology, 1986We have examined the murine cell-mediated immune (CMI) response to collagens type I (CI) and type II (CII) as measured by in vivo delayed-type hypersensitivity responses. We have verified the histopathology and kinetics of the cell-mediated immune responses. Predominant cell-mediated responses were obtained 7, 10, or 14 days following immunization.
L, Butler +4 more
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Structure of equine type I and type II collagens
American Journal of Veterinary Research, 1994Summary Collagen type I was purified from equine skin and flexor tendon, and type II collagen was purified from equine articular cartilage. The proteoglycans in these tissues were extracted, using guanidine hcl; the collagens were solubilized, using pepsin digestion, then were selectively precipitated with NaCl.
R J, Todhunter +3 more
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Matrix Biology, 2006
The objective of this study was to determine whether a fragment(s) of type II collagen can induce cartilage degradation. Fragments generated by cyanogen bromide (CB) cleavage of purified bovine type II collagen were separated by HPLC. These fragments together with selected overlapping synthetic peptides were first analysed for their capacity to induce ...
Tadashi, Yasuda +8 more
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The objective of this study was to determine whether a fragment(s) of type II collagen can induce cartilage degradation. Fragments generated by cyanogen bromide (CB) cleavage of purified bovine type II collagen were separated by HPLC. These fragments together with selected overlapping synthetic peptides were first analysed for their capacity to induce ...
Tadashi, Yasuda +8 more
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Archives of Oral Biology, 1995
Sprague-Dawley rats (50 days old) were anaesthetized and the maxillary right molars extracted. The rats were killed at 2, 3, 6, 8 and 10 days after extraction. The maxillae were dissected and prepared for either routine histology, in situ hybridization for pro-collagen type II mRNA, or immunohistochemical detection of collagen type II.
Devlin, H.; id_orcid 0000-0002-5120-747X +3 more
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Sprague-Dawley rats (50 days old) were anaesthetized and the maxillary right molars extracted. The rats were killed at 2, 3, 6, 8 and 10 days after extraction. The maxillae were dissected and prepared for either routine histology, in situ hybridization for pro-collagen type II mRNA, or immunohistochemical detection of collagen type II.
Devlin, H.; id_orcid 0000-0002-5120-747X +3 more
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