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Human LDH-A4 and rat LDH-A4 together are a good example of?

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Final answer:

LDH-A4 is an isoenzyme form of lactate dehydrogenase found in both humans and rats. It exhibits different physical characteristics and is distributed differently in different species, reflecting evolutionary adaptations.

Step-by-step explanation:

LDH-A4 is an isoenzyme form of lactate dehydrogenase found in both humans and rats. It is an example of multiple forms of the same enzyme that exhibit different physical characteristics. In humans, LDH-A4 is predominantly present in the cardiac muscle, while in rats, it is more abundant in the skeletal muscle. These differences in distribution and characteristics of LDH-A4 highlight the evolutionary adaptations in different species.

Human LDH-A4 and rat LDH-A4 demonstrate evolutionary homology, as they are example of similar genetic traits found in different species due to common ancestry. These enzymes are part of a complex system of isoenzymes that have evolved to fulfill specialized metabolic functions and are used as diagnostic markers for tissue damage in medical settings.

Human LDH-A4 and rat LDH-A4 are a good example of evolutionary homology. These enzymes represent how organisms from different species can share similar genetic traits due to common ancestry. The enzyme lactate dehydrogenase (LDH) exists in multiple isoenzyme forms, specifically as tetramers made up of 'H chain' and 'M chain' polypeptides. These forms vary across different species and tissue types, reflecting their evolutionary adaptation to specific metabolic requirements.

In the context of evolutionary biology, the variety within LDH isoforms in different species including the human LDH-A4 and rat LDH-A4 can be mapped out on a cladogram to illustrate their evolutionary relationships. The evolutionary sequence of LDH isoenzymes (LDH-A, -B, and -C) can be analyzed and compared to understand the likely paths of evolution among different species, such as in the African frog and in humans. The different Km values of these isoenzymes explain their varying affinities for substrates like pyruvate, implicating their specialized roles in metabolism.

Moreover, specific isoenzymes are used as markers in medical diagnostics for tissue damage and disease. For example, an elevated level of LDH5, which is an M4 isoenzyme, indicates liver damage, while myocardial infarction is characterized by high levels of LDH1, an H4 isoenzyme.

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