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- W2018100890 abstract "The thermal stability of the helical domain of intracellular and matrix-associated type X̄ collagen was examined in situ within the hypertrophic region of embryonic chick vertebral cartilages. For this we employed indirect immunofluorescence histochemistry of unfixed tissue sections reacted at progressively higher temperatures (Linsenmayer et al., J cell biol 99 (1984) 1405) [18] with a conformation-dependent monoclonal antibody (X̄-AC9) (Schmid & Linsenmayer, J cell biol 100 (1985) 598) [19]. The hypertrophic chondrocytes which had most recently initiated synthesis of type X̄ did not immediately secrete it, but instead retained it intracellularly within cytoplasmic organelles. This allowed for clear visualization of the intracellular type X̄. Within the pool of intracellular type X̄ collagen, the epitope recognized by the antibody was stable up to 55 °C, but was destroyed at 60 °C. This is 5–10 °C higher than the thermal stability of the epitope when the molecule is in neutral solution (as determined by competition ELISA). The matrix-associated type X̄ collagen is stable at least to 65–67.5 °C. We conclude that in situ the stability of the collagen helix in its normal intracellular environment is considerably greater than might be predicted from measurements made on molecules in solution." @default.
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- W2018100890 title "Intracellular avian type X collagen in situ and determination of its thermal stability using a conformation-dependent monoclonal antibody" @default.
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- W2018100890 doi "https://doi.org/10.1016/0014-4827(86)90504-5" @default.
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