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Nesterboy [21]
3 years ago
10

Some cells release active signaling proteins when membrane-bound precursor proteins are cleaved by proteolytic enzymes. The sign

aling proteins can then bind to receptors on the surface of a target cell, thereby activating an intracellular signaling pathway and eliciting a response from the target cell. This mechanism of activating receptor-binding signaling proteins has been observed in a variety of organisms from bacteria to humans. Many of the enzymes responsible for proteolysis of membrane-bound precursor proteins have been isolated and characterized.
Required:

What questions would be most appropriate to investigate whether the proteolytic enzymes are evolutionarily conserved among species?
Biology
1 answer:
Tcecarenko [31]3 years ago
6 0

Answer:

Following questions would be most appropriate to investigate whether the proteolytic enzymes are evolutionarily conserved among species:

  1. Are the genes encoding the proteolytic enzymes expressed in the same cell types in all species?  
  2. Once the precursor proteins of different species are cleaved, do the active signaling proteins bind to  the same receptors on different target cells?
  3. If a proteolytic enzyme from one species is incubated with a precursor protein from another species, does correct cleavage occur?
  4. Are the proteolytic enzymes synthesized in the rough endoplasmic reticulum of all species?
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Parasites are classified as ectoparasites, which live on the body surface of the host (ticks, fleas, leeches, and lice) and endoparasites, which live in the body of the host. Endoparasites are either intercellular, which live inside the host’s body (round worms, tapeworms) or intracellular, which live inside the cells in the host’s body (bacteria or viruses).

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