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使用戊二醛和鞣酸保存用于电子显微镜检查的重组胶原蛋白。

The use of glutaraldehyde and tannic acid to preserve reconstituted collagen for electron microscopy.

作者信息

Meek K M

出版信息

Histochemistry. 1981;73(1):115-20. doi: 10.1007/BF00493137.

DOI:10.1007/BF00493137
PMID:6797991
Abstract

The effects of glutaraldehyde and tannic acid on the axial periodicity of collagen have measured. Both fixatives produce axial shrinkage of the collagen but whereas glutaraldehyde produces 7% shrinkage, tannic acid produces only 2% shrinkage. The technique of carbon/platinum shadowing was used to estimate the extent to which the collagen fibrils flatten down when they are dried onto grids for electron microscopy without prior embedding and sectioning. The influence of fixation was studied and it was found that minimum distortion occurred when both tannic acid and glutaraldehyde were used to preserve the protein structure.

摘要

已测量戊二醛和单宁酸对胶原蛋白轴向周期性的影响。两种固定剂都会使胶原蛋白产生轴向收缩,但戊二醛产生7%的收缩,而单宁酸仅产生2%的收缩。采用碳/铂阴影技术来估计胶原蛋白纤维在未经预先包埋和切片而干燥到用于电子显微镜观察的网格上时变平的程度。研究了固定的影响,发现使用单宁酸和戊二醛来保存蛋白质结构时产生的变形最小。

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The staining pattern of collagen fibrils. II. A comparison with patterns computer-generated from the amino acid sequence.
Connect Tissue Res. 1974;2(2):151-9. doi: 10.3109/03008207409152100.
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Connect Tissue Res. 1974;2(2):137-50. doi: 10.3109/03008207409152099.
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Differential fixation of poly(L-arginine) and poly(L-lysine) by tannic acid and its application to the fixation of collagen in electron microscopy.单宁酸对聚(L-精氨酸)和聚(L-赖氨酸)的差异固定作用及其在电子显微镜下对胶原蛋白固定的应用。
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