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. 2021 May 17;53(6):917–928. doi: 10.1007/s00726-021-02994-w

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© The Author(s) 2021

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 6 — Comparison of scatter in frozen and lyophilized, pulverized samples from fibrotic kidneys. a Representative Masson's trichrome-stained sections of diabetic rat kidneys. Arrows show examples of focal fibrosis. (10–200 × magnification, scale bar = 2000 μm, 50 μm.) b Absolute differences of alpha smooth muscle actin protein (αSMA) values to mean in diabetic rat kidneys processed conventionally (Frozen) or homogenized after lyophilization (n = 10/group). c Schematic presentation of sample processing for homogeneity investigations. One half of each kidney was lyophilized (L) and pulverized, protein and RNA were isolated four times from homogenous powder (L1–L4). The other half went through conventional frozen sample processing; four pieces were cut for the isolations (F1–F4). d Absolute differences of αSMA protein and e alpha smooth muscle actin mRNA (Acta2) values to mean in frozen parts vs. lyophilized homogenous powder of the same diabetic rat kidney samples (n = 4 frozen parts and 4 powder portions of the same kidneys)