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- BookManfred Dietel, Christian Wittekind, Gianni Bussolati, Moritz von Winterfeld, editors.Summary: This book presents an overview of the most important current developments in the pre-analytical handling of tissue. It addresses in particular potential ways to improve the situation whereby methods employed in the pre-analytical phase ? the period from surgical removal of tissue to the start of pathological processing ? have remained essentially unchanged for decades with only modest standardization. It is examined how the pre-analytical period can be optimized, resulting not only in an increase in diagnostic quality but also in a reduction in processing time and costs. Among the key topics examined are the so-called cold ischemia time between tissue removal and fixation, the potential superiority of vacuum-based preservation over immediate formalin fixation, two-temperature fixation, molecular analysis methods, and the pre-analytics of specimens from particular tissues. Readers will find this book to be an important update that reveals the full importance of the pre-analytical phase for quality of pathological work-up.
Contents:
What Is Pre-Analytics in Surgical Pathology?
Histologic Validation of Vacuum Sealed Formalin
Free Tissue Preservation and Transport System
Pre-Analytics and Molecular Pathology
Experiences in Vacuum Preparation of Routine Specimens
Tissue Heterogeneity as a Pre-Analytical Source of Variability
Vacuum Fixation of Breast Specimens Before Grossing
How Do Short Fixation and Rapid Microwave Processing Affect Her2 Testing?
Current Projects in Pre-Analytics ? Where to Go?
Nucleic Acid Extraction from FFPE Tissue as Critical Preanalytic Step for NGS Applications
Experiences With Pre-Analytics of Lung Specimen
Experiences With Pre-Analytics of GI-Specimen
Bone Marrow Work-Up
Two-Temperature Fixation Preserves Activation Status with High Efficiency
Towards the Lean Lab. The Industry Challenge. . - ArticleLeĭbman DIa, Nesterov VP.Biokhimiia. 1979 May;44(5):822-31.The purified preparations of glyceraldehyde-3-phosphate dehydrogenase isolated from frog and pike skeletal muscles were found homogenous under polyacrylamide gel electrophoresis. Their amino acid composition is similar to that of glyceraldehyde-3-phosphate dehydrogenase from other animal species. The interaction kinetics for frog and pike glyceraldehyde-3-phosphate dehydrogenase SH-groups with 5,5'-dithio-bis-(2-nitrobenzoate) (DTNB) were studied. A negative correlation between the thermal stability of the enzyme preparations from pig, pike, lamprey and frog muscles and the reactivity of their SH-groups with respect to DTNB was observed. NAD at saturating concentrations was found to protect the enzyme from lower vertebrates muscles against thermal inactivation in a lesser degree than does the pig muscle enzyme. The weaker protective effect of NAD was observed for lamprey and frog enzyme preparations, which are characterized by a low SH-group reaction ability. Frog and pike apoenzymes are considerably more resistant to trypsin proteolysis than the pig apoenzyme.