Cytophotometry of post mortem glycogenolysis in quiescent bovine muscle fibres in relation to temperature, succinate dehydrogenase activity and adenosine triphosphatase activity. 1980

H J Swatland

Immediate post mortem samples of sternomandibularis muscles from six steers were maintained with a minimum of intrinsic activity at approximately 40 degrees C or allowed to cool to approximately 22 degrees C. Samples were frozen in liquid nitrogen at 0, 2, 4 and 6 h post mortem and serial transverse sections were stained by the periodic acid-Schiff (PAS) reaction for glycogen or reacted for adenosine triphosphatase (ATPase) or succinate dehydrogenase. Individual fibres were mapped and categorized from their ATPase and succinate dehydrogenase activity using a projecting microscope. The absorbance of PAS-stained glycogen in individual fibres was measured with a microscope photometer at 570 and 601 nm with a correction for distributional error. Overall, the post mortem decline in absorbance was approximately twice as fast in body temperature samples relative to room temperature samples. Transient post mortem increases in absorbance were detected in some situations, particularly in fibres with strong ATPase activity from room temperature samples. In fibres with strong ATPase activity, the rate of decline in absorbance increased progressively post mortem. Fibres with weak ATPase mostly had a lower initial post mortem absorbance and were generally the first to become PAS-negative.

UI MeSH Term Description Entries
D008297 Male Males
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D010503 Periodic Acid-Schiff Reaction A histochemical technique for staining carbohydrates. It is based on PERIODIC ACID oxidation of a substance containing adjacent hydroxyl groups. The resulting aldehydes react with Schiff reagent to form a colored product. PAS Reaction,PAS Reactions,Periodic Acid Schiff Reaction,Periodic Acid-Schiff Reactions,Reaction, PAS,Reaction, Periodic Acid-Schiff,Reactions, PAS,Reactions, Periodic Acid-Schiff
D011180 Postmortem Changes Physiological changes that occur in bodies after death. Adipocere,Algor Mortis,Cruor,Livor Mortis,Change, Postmortem,Changes, Postmortem,Postmortem Change
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D006003 Glycogen
D006651 Histocytochemistry Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods. Cytochemistry
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013385 Succinate Dehydrogenase A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II. Succinic Oxidase,Fumarate Reductase,Succinic Dehydrogenase,Dehydrogenase, Succinate,Dehydrogenase, Succinic,Oxidase, Succinic,Reductase, Fumarate
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